2aec - Revision history

OCA at 07:33, 9 October 2024

2024-10-09T07:33:45Z

← Older revision		Revision as of 07:33, 9 October 2024
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	<StructureSection load='2aec' size='340' side='right'caption='[[2aec]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='2aec' size='340' side='right'caption='[[2aec]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>~~[[2aec]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens].~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AEC FirstGlance]. <br>		<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AEC FirstGlance]. <br>
	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2Å</td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2Å</td></tr>
	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5-DIPHOSPHATE'>UDH</scene></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5-DIPHOSPHATE'>UDH</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [https://pdbe.org/2aec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [https://www.ebi.ac.uk/pdbsum/2aec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aec ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [https://pdbe.org/2aec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [https://www.ebi.ac.uk/pdbsum/2aec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aec ProSAT]</span></td></tr>
	</table>		</table>
	~~== Disease ==~~
	[https://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN] Defects in B4GALT1 are the cause of congenital disorder of glycosylation type 2D (CDG2D) [MIM:[https://omim.org/entry/607091 607091]. CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
	~~== Function ==~~
	[https://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN] The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/2aec_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/2aec_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Homo sapiens]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Boeggeman E]]		[[Category: Boeggeman E]]

OCA at 07:22, 23 August 2023

2023-08-23T07:22:56Z

← Older revision		Revision as of 07:22, 23 August 2023
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	<StructureSection load='2aec' size='340' side='right'caption='[[2aec]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='2aec' size='340' side='right'caption='[[2aec]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2aec]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AEC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2aec]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AEC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=~~SO4~~:~~SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6~~-~~AMINOHEXYL~~-~~URIDINE~~-~~C1,5-DIPHOSPHATE~~'>~~UDH~~</scene>, <scene name='pdbligand=~~MAN~~:~~ALPHA-D-MANNOSE~~'>~~MAN~~</scene>, <scene name='pdbligand=~~NAG~~:N-~~ACETYL~~-D-~~GLUCOSAMINE'>NAG</scene></td></tr>~~		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2Å</td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1o0r\|1o0r]], [[1tvy\|1tvy]], [[1tw1\|1tw1]], [[1tw5\|1tw5]], [[2ae7\|2ae7]], [[2aes\|2aes]], [[2agd\|2agd]], [[2ah9\|2ah9]]</div></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5-DIPHOSPHATE'>UDH</scene></td></tr>
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B4GALT1~~, ~~GGTB2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=~~5~~&id=9606 HUMAN])</td></tr>~~
	~~<tr id='activity~~'>~~<td class="sblockLbl"><b>Activity:~~</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N-acetyllactosamine_synthase N-acetyllactosamine synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.90 2.4.1.90] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [https://pdbe.org/2aec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [https://www.ebi.ac.uk/pdbsum/2aec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aec ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [https://pdbe.org/2aec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [https://www.ebi.ac.uk/pdbsum/2aec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aec ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] Defects in B4GALT1 are the cause of congenital disorder of glycosylation type 2D (CDG2D) [MIM:[https://omim.org/entry/607091 607091]]. CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.		[https://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN] Defects in B4GALT1 are the cause of congenital disorder of glycosylation type 2D (CDG2D) [MIM:[https://omim.org/entry/607091 607091]. CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.		[https://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN] The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[Category: N-acetyllactosamine synthase]]~~		[[Category: Boeggeman E]]
	[[Category: Boeggeman, E]]		[[Category: Qasba PK]]
	[[Category: Qasba~~, P K~~]]		[[Category: Ramakrishnan B]]
	[[Category: Ramakrishnan, B]]		[[Category: Ramasamy V]]
	[[Category: Ramasamy, V]]		[[Category: Ratner DM]]
	[[Category: Ratner~~, D M~~]]		[[Category: Seeberger PH]]
	[[Category: Seeberger~~, P H]]~~
	~~[[Category: 4-galactosyltransferase-i]]~~
	~~[[Category: Beta1]]~~
	~~[[Category: Closed conformation]]~~
	~~[[Category: Mutant]]~~
	~~[[Category: Transferase]]~~
	~~[[Category: Trisaccharide~~]]

OCA at 17:08, 20 October 2021

2021-10-20T17:08:49Z

← Older revision		Revision as of 17:08, 20 October 2021
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	==Crystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4GAL-T1) in Complex with GlcNAc-beta1,2-Man-alpha1,6-Man-beta-OR==		==Crystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4GAL-T1) in Complex with GlcNAc-beta1,2-Man-alpha1,6-Man-beta-OR==
	<StructureSection load='2aec' size='340' side='right'caption='[[2aec]]' scene=''>		<StructureSection load='2aec' size='340' side='right'caption='[[2aec]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AEC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2aec]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AEC FirstGlance]. <br>
	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [https://pdbe.org/2aec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [https://www.ebi.ac.uk/pdbsum/2aec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aec ProSAT]</span></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5-DIPHOSPHATE'>UDH</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1o0r\|1o0r]], [[1tvy\|1tvy]], [[1tw1\|1tw1]], [[1tw5\|1tw5]], [[2ae7\|2ae7]], [[2aes\|2aes]], [[2agd\|2agd]], [[2ah9\|2ah9]]</div></td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B4GALT1, GGTB2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N-acetyllactosamine_synthase N-acetyllactosamine synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.90 2.4.1.90] </span></td></tr>
			<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [https://pdbe.org/2aec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [https://www.ebi.ac.uk/pdbsum/2aec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aec ProSAT]</span></td></tr>
	</table>		</table>
			== Disease ==
			[[https://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] Defects in B4GALT1 are the cause of congenital disorder of glycosylation type 2D (CDG2D) [MIM:[https://omim.org/entry/607091 607091]]. CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
			== Function ==
			[[https://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 16:		Line 24:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2aec ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2aec ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			beta-1,4-Galactosyltransferase-I (beta4Gal-T1) transfers galactose from UDP-galactose to N-acetylglucosamine (GlcNAc) residues of the branched N-linked oligosaccharide chains of glycoproteins. In an N-linked biantennary oligosaccharide chain, one antenna is attached to the 3-hydroxyl-(1,3-arm), and the other to the 6-hydroxyl-(1,6-arm) group of mannose, which is beta-1,4-linked to an N-linked chitobiose, attached to the aspargine residue of a protein. For a better understanding of the branch specificity of beta4Gal-T1 towards the GlcNAc residues of N-glycans, we have carried out kinetic and crystallographic studies with the wild-type human beta4Gal-T1 (h-beta4Gal-T1) and the mutant Met340His-beta4Gal-T1 (h-M340H-beta4Gal-T1) in complex with a GlcNAc-containing pentasaccharide and several GlcNAc-containing trisaccharides present in N-glycans. The oligosaccharides used were: pentasaccharide GlcNAcbeta1,2-Manalpha1,6 (GlcNAcbeta1,2-Manalpha1,3)Man; the 1,6-arm trisaccharide, GlcNAcbeta1,2-Manalpha1,6-Manbeta-OR (1,2-1,6-arm); the 1,3-arm trisaccharides, GlcNAcbeta1,2-Manalpha1,3-Manbeta-OR (1,2-1,3-arm) and GlcNAcbeta1,4-Manalpha1,3-Manbeta-OR (1,4-1,3-arm); and the trisaccharide GlcNAcbeta1,4-GlcNAcbeta1,4-GlcNAc (chitotriose). With the wild-type h-beta4Gal-T1, the K(m) of 1,2-1,6-arm is approximately tenfold lower than for 1,2-1,3-arm and 1,4-1,3-arm, and 22-fold lower than for chitotriose. Crystal structures of h-M340H-beta4Gal-T1 in complex with the pentasaccharide and various trisaccharides at 1.9-2.0A resolution showed that beta4Gal-T1 is in a closed conformation with the oligosaccharide bound to the enzyme, and the 1,2-1,6-arm trisaccharide makes the maximum number of interactions with the enzyme, which is in concurrence with the lowest K(m) for the trisaccharide. Present studies suggest that beta4Gal-T1 interacts preferentially with the 1,2-1,6-arm trisaccharide rather than with the 1,2-1,3-arm or 1,4-1,3-arm of a bi- or tri-antennary oligosaccharide chain of N-glycan.

			Oligosaccharide preferences of beta1,4-galactosyltransferase-I: crystal structures of Met340His mutant of human beta1,4-galactosyltransferase-I with a pentasaccharide and trisaccharides of the N-glycan moiety.,Ramasamy V, Ramakrishnan B, Boeggeman E, Ratner DM, Seeberger PH, Qasba PK J Mol Biol. 2005 Oct 14;353(1):53-67. PMID:16157350<ref>PMID:16157350</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 2aec" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Glycosyltransferase 3D structures\|Glycosyltransferase 3D structures]]		*[[Glycosyltransferase 3D structures\|Glycosyltransferase 3D structures]]
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Boeggeman E]]		[[Category: N-acetyllactosamine synthase]]
	[[Category: Qasba PK]]		[[Category: Boeggeman, E]]
	[[Category: Ramakrishnan B]]		[[Category: Qasba, P K]]
	[[Category: Ramasamy V]]		[[Category: Ramakrishnan, B]]
	[[Category: Ratner DM]]		[[Category: Ramasamy, V]]
	[[Category: Seeberger PH]]		[[Category: Ratner, D M]]
			[[Category: Seeberger, P H]]
			[[Category: 4-galactosyltransferase-i]]
			[[Category: Beta1]]
			[[Category: Closed conformation]]
			[[Category: Mutant]]
			[[Category: Transferase]]
			[[Category: Trisaccharide]]

OCA at 11:31, 3 February 2021

2021-02-03T11:31:22Z

← Older revision		Revision as of 11:31, 3 February 2021
Line 1:		Line 1:

	==Crystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4GAL-T1) in Complex with GlcNAc-beta1,2-Man-alpha1,6-Man-beta-OR==		==Crystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4GAL-T1) in Complex with GlcNAc-beta1,2-Man-alpha1,6-Man-beta-OR==
	<StructureSection load='2aec' size='340' side='right' caption='[[2aec]]~~, [[Resolution\|resolution]] 2.00Å~~' scene=''>		<StructureSection load='2aec' size='340' side='right'caption='[[2aec]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>~~[[2aec]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human].~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2AEC FirstGlance]. <br>		<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AEC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5-DIPHOSPHATE'>UDH</scene></td></tr>		</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [https://pdbe.org/2aec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [https://www.ebi.ac.uk/pdbsum/2aec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aec ProSAT]</span></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0r\|1o0r]], [[1tvy\|1tvy]], [[1tw1\|1tw1]], [[1tw5\|1tw5]], [[2ae7\|2ae7]], [[2aes\|2aes]], [[2agd\|2agd]], [[2ah9\|2ah9]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B4GALT1, GGTB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetyllactosamine_synthase N-acetyllactosamine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.90 2.4.1.90] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [~~http~~://pdbe.org/2aec PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2aec PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2aec ProSAT]</span></td></tr>
	</table>		</table>
	~~== Disease ==~~
	[[http://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] Defects in B4GALT1 are the cause of congenital disorder of glycosylation type 2D (CDG2D) [MIM:[http://omim.org/entry/607091 607091]]. CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
	~~== Function ==~~
	[[http://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 24:		Line 16:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2aec ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2aec ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	beta-1,4-Galactosyltransferase-I (beta4Gal-T1) transfers galactose from UDP-galactose to N-acetylglucosamine (GlcNAc) residues of the branched N-linked oligosaccharide chains of glycoproteins. In an N-linked biantennary oligosaccharide chain, one antenna is attached to the 3-hydroxyl-(1,3-arm), and the other to the 6-hydroxyl-(1,6-arm) group of mannose, which is beta-1,4-linked to an N-linked chitobiose, attached to the aspargine residue of a protein. For a better understanding of the branch specificity of beta4Gal-T1 towards the GlcNAc residues of N-glycans, we have carried out kinetic and crystallographic studies with the wild-type human beta4Gal-T1 (h-beta4Gal-T1) and the mutant Met340His-beta4Gal-T1 (h-M340H-beta4Gal-T1) in complex with a GlcNAc-containing pentasaccharide and several GlcNAc-containing trisaccharides present in N-glycans. The oligosaccharides used were: pentasaccharide GlcNAcbeta1,2-Manalpha1,6 (GlcNAcbeta1,2-Manalpha1,3)Man; the 1,6-arm trisaccharide, GlcNAcbeta1,2-Manalpha1,6-Manbeta-OR (1,2-1,6-arm); the 1,3-arm trisaccharides, GlcNAcbeta1,2-Manalpha1,3-Manbeta-OR (1,2-1,3-arm) and GlcNAcbeta1,4-Manalpha1,3-Manbeta-OR (1,4-1,3-arm); and the trisaccharide GlcNAcbeta1,4-GlcNAcbeta1,4-GlcNAc (chitotriose). With the wild-type h-beta4Gal-T1, the K(m) of 1,2-1,6-arm is approximately tenfold lower than for 1,2-1,3-arm and 1,4-1,3-arm, and 22-fold lower than for chitotriose. Crystal structures of h-M340H-beta4Gal-T1 in complex with the pentasaccharide and various trisaccharides at 1.9-2.0A resolution showed that beta4Gal-T1 is in a closed conformation with the oligosaccharide bound to the enzyme, and the 1,2-1,6-arm trisaccharide makes the maximum number of interactions with the enzyme, which is in concurrence with the lowest K(m) for the trisaccharide. Present studies suggest that beta4Gal-T1 interacts preferentially with the 1,2-1,6-arm trisaccharide rather than with the 1,2-1,3-arm or 1,4-1,3-arm of a bi- or tri-antennary oligosaccharide chain of N-glycan.

	Oligosaccharide preferences of beta1,4-galactosyltransferase-I: crystal structures of Met340His mutant of human beta1,4-galactosyltransferase-I with a pentasaccharide and trisaccharides of the N-glycan moiety.,Ramasamy V, Ramakrishnan B, Boeggeman E, Ratner DM, Seeberger PH, Qasba PK J Mol Biol. 2005 Oct 14;353(1):53-67. PMID:16157350<ref>PMID:16157350</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2aec" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Glycosyltransferase\|Glycosyltransferase]]		*[[Glycosyltransferase 3D structures\|Glycosyltransferase 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human]]~~		[[Category: Large Structures]]
	~~[[Category: N-acetyllactosamine synthase~~]]		[[Category: Boeggeman E]]
	[[Category: Boeggeman, E]]		[[Category: Qasba PK]]
	[[Category: Qasba~~, P K~~]]		[[Category: Ramakrishnan B]]
	[[Category: Ramakrishnan, B]]		[[Category: Ramasamy V]]
	[[Category: Ramasamy, V]]		[[Category: Ratner DM]]
	[[Category: Ratner~~, D M~~]]		[[Category: Seeberger PH]]
	[[Category: Seeberger~~, P H]]~~
	~~[[Category: 4-galactosyltransferase-i]]~~
	~~[[Category: Beta1]]~~
	~~[[Category: Closed conformation]]~~
	~~[[Category: Mutant]]~~
	~~[[Category: Transferase]]~~
	~~[[Category: Trisaccharide~~]]

OCA at 06:47, 9 May 2018

2018-05-09T06:47:33Z

← Older revision		Revision as of 06:47, 9 May 2018
Line 1:		Line 1:

	==Crystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4GAL-T1) in Complex with GlcNAc-beta1,2-Man-alpha1,6-Man-beta-OR==		==Crystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4GAL-T1) in Complex with GlcNAc-beta1,2-Man-alpha1,6-Man-beta-OR==
	<StructureSection load='2aec' size='340' side='right' caption='[[2aec]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='2aec' size='340' side='right' caption='[[2aec]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2aec]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AEC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2aec]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AEC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=~~SO4~~:~~SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6~~-~~AMINOHEXYL~~-~~URIDINE~~-~~C1,5-DIPHOSPHATE~~'>~~UDH~~</scene>, <scene name='pdbligand=~~MAN~~:~~ALPHA-D-MANNOSE~~'>~~MAN~~</scene>, <scene name='pdbligand=~~NAG~~:N-~~ACETYL~~-D-~~GLUCOSAMINE~~'>~~NAG~~</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5-DIPHOSPHATE'>UDH</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0r\|1o0r]], [[1tvy\|1tvy]], [[1tw1\|1tw1]], [[1tw5\|1tw5]], [[2ae7\|2ae7]], [[2aes\|2aes]], [[2agd\|2agd]], [[2ah9\|2ah9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0r\|1o0r]], [[1tvy\|1tvy]], [[1tw1\|1tw1]], [[1tw5\|1tw5]], [[2ae7\|2ae7]], [[2aes\|2aes]], [[2agd\|2agd]], [[2ah9\|2ah9]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B4GALT1, GGTB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B4GALT1, GGTB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetyllactosamine_synthase N-acetyllactosamine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.90 2.4.1.90] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetyllactosamine_synthase N-acetyllactosamine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.90 2.4.1.90] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [http://pdbe.org/2aec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [http://www.ebi.ac.uk/pdbsum/2aec PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [http://pdbe.org/2aec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [http://www.ebi.ac.uk/pdbsum/2aec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2aec ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 17:		Line 18:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/2aec_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/2aec_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 18:03, 7 February 2016

2016-02-07T18:03:32Z

← Older revision		Revision as of 18:03, 7 February 2016
Line 21:		Line 21:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2aec ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 03:52, 10 September 2015

2015-09-10T03:52:29Z

← Older revision		Revision as of 03:52, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='2aec' size='340' side='right' caption='[[2aec]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='2aec' size='340' side='right' caption='[[2aec]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2aec]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AEC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2aec]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AEC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5-DIPHOSPHATE'>UDH</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5-DIPHOSPHATE'>UDH</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0r\|1o0r]], [[1tvy\|1tvy]], [[1tw1\|1tw1]], [[1tw5\|1tw5]], [[2ae7\|2ae7]], [[2aes\|2aes]], [[2agd\|2agd]], [[2ah9\|2ah9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0r\|1o0r]], [[1tvy\|1tvy]], [[1tw1\|1tw1]], [[1tw5\|1tw5]], [[2ae7\|2ae7]], [[2aes\|2aes]], [[2agd\|2agd]], [[2ah9\|2ah9]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B4GALT1, GGTB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B4GALT1, GGTB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetyllactosamine_synthase N-acetyllactosamine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.90 2.4.1.90] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetyllactosamine_synthase N-acetyllactosamine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.90 2.4.1.90] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [http://www.ebi.ac.uk/pdbsum/2aec PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [http://pdbe.org/2aec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [http://www.ebi.ac.uk/pdbsum/2aec PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 31:		Line 31:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 2aec" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 39:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: N-acetyllactosamine synthase]]		[[Category: N-acetyllactosamine synthase]]
	[[Category: Boeggeman, E]]		[[Category: Boeggeman, E]]

OCA at 08:55, 8 January 2015

2015-01-08T08:55:16Z

← Older revision		Revision as of 08:55, 8 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2aec]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AEC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2aec]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AEC FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5-DIPHOSPHATE'>UDH</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5-DIPHOSPHATE'>UDH</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0r\|1o0r]], [[1tvy\|1tvy]], [[1tw1\|1tw1]], [[1tw5\|1tw5]], [[2ae7\|2ae7]], [[2aes\|2aes]], [[2agd\|2agd]], [[2ah9\|2ah9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0r\|1o0r]], [[1tvy\|1tvy]], [[1tw1\|1tw1]], [[1tw5\|1tw5]], [[2ae7\|2ae7]], [[2aes\|2aes]], [[2agd\|2agd]], [[2ah9\|2ah9]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B4GALT1, GGTB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B4GALT1, GGTB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetyllactosamine_synthase N-acetyllactosamine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.90 2.4.1.90] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetyllactosamine_synthase N-acetyllactosamine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.90 2.4.1.90] </span></td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [http://www.ebi.ac.uk/pdbsum/2aec PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [http://www.ebi.ac.uk/pdbsum/2aec PDBsum]</span></td></tr>
	<table>		</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] Defects in B4GALT1 are the cause of congenital disorder of glycosylation type 2D (CDG2D) [MIM:[http://omim.org/entry/607091 607091]]. CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.		[[http://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] Defects in B4GALT1 are the cause of congenital disorder of glycosylation type 2D (CDG2D) [MIM:[http://omim.org/entry/607091 607091]]. CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
Line 40:		Line 40:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: N-acetyllactosamine synthase]]		[[Category: N-acetyllactosamine synthase]]
	[[Category: Boeggeman, E.]]		[[Category: Boeggeman, E]]
	[[Category: Qasba, P K.]]		[[Category: Qasba, P K]]
	[[Category: Ramakrishnan, B.]]		[[Category: Ramakrishnan, B]]
	[[Category: Ramasamy, V.]]		[[Category: Ramasamy, V]]
	[[Category: Ratner, D M.]]		[[Category: Ratner, D M]]
	[[Category: Seeberger, P H.]]		[[Category: Seeberger, P H]]
	[[Category: 4-galactosyltransferase-i]]		[[Category: 4-galactosyltransferase-i]]
	[[Category: Beta1]]		[[Category: Beta1]]

OCA at 23:48, 29 September 2014

2014-09-29T23:48:52Z

← Older revision		Revision as of 23:48, 29 September 2014
Line 1:		Line 1:
	~~{{STRUCTURE_2aec\| PDB=2aec \| SCENE= }}~~		==Crystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4GAL-T1) in Complex with GlcNAc-beta1,2-Man-alpha1,6-Man-beta-OR==
	===Crystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4GAL-T1) in Complex with GlcNAc-beta1,2-Man-alpha1,6-Man-beta-OR===		<StructureSection load='2aec' size='340' side='right' caption='[[2aec]], [[Resolution\|resolution]] 2.00Å' scene=''>
	~~{{ABSTRACT_PUBMED_16157350}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[2aec]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AEC FirstGlance]. <br>
	==Disease==		</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5-DIPHOSPHATE'>UDH</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0r\|1o0r]], [[1tvy\|1tvy]], [[1tw1\|1tw1]], [[1tw5\|1tw5]], [[2ae7\|2ae7]], [[2aes\|2aes]], [[2agd\|2agd]], [[2ah9\|2ah9]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B4GALT1, GGTB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetyllactosamine_synthase N-acetyllactosamine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.90 2.4.1.90] </span></td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2aec RCSB], [http://www.ebi.ac.uk/pdbsum/2aec PDBsum]</span></td></tr>
			<table>
			== Disease ==
	[[http://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] Defects in B4GALT1 are the cause of congenital disorder of glycosylation type 2D (CDG2D) [MIM:[http://omim.org/entry/607091 607091]]. CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.		[[http://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] Defects in B4GALT1 are the cause of congenital disorder of glycosylation type 2D (CDG2D) [MIM:[http://omim.org/entry/607091 607091]]. CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
			== Function ==
			[[http://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/2aec_consurf.spt"</scriptWhenChecked>
			<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
			<text>to colour the structure by Evolutionary Conservation</text>
			</jmolCheckbox>
			</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			beta-1,4-Galactosyltransferase-I (beta4Gal-T1) transfers galactose from UDP-galactose to N-acetylglucosamine (GlcNAc) residues of the branched N-linked oligosaccharide chains of glycoproteins. In an N-linked biantennary oligosaccharide chain, one antenna is attached to the 3-hydroxyl-(1,3-arm), and the other to the 6-hydroxyl-(1,6-arm) group of mannose, which is beta-1,4-linked to an N-linked chitobiose, attached to the aspargine residue of a protein. For a better understanding of the branch specificity of beta4Gal-T1 towards the GlcNAc residues of N-glycans, we have carried out kinetic and crystallographic studies with the wild-type human beta4Gal-T1 (h-beta4Gal-T1) and the mutant Met340His-beta4Gal-T1 (h-M340H-beta4Gal-T1) in complex with a GlcNAc-containing pentasaccharide and several GlcNAc-containing trisaccharides present in N-glycans. The oligosaccharides used were: pentasaccharide GlcNAcbeta1,2-Manalpha1,6 (GlcNAcbeta1,2-Manalpha1,3)Man; the 1,6-arm trisaccharide, GlcNAcbeta1,2-Manalpha1,6-Manbeta-OR (1,2-1,6-arm); the 1,3-arm trisaccharides, GlcNAcbeta1,2-Manalpha1,3-Manbeta-OR (1,2-1,3-arm) and GlcNAcbeta1,4-Manalpha1,3-Manbeta-OR (1,4-1,3-arm); and the trisaccharide GlcNAcbeta1,4-GlcNAcbeta1,4-GlcNAc (chitotriose). With the wild-type h-beta4Gal-T1, the K(m) of 1,2-1,6-arm is approximately tenfold lower than for 1,2-1,3-arm and 1,4-1,3-arm, and 22-fold lower than for chitotriose. Crystal structures of h-M340H-beta4Gal-T1 in complex with the pentasaccharide and various trisaccharides at 1.9-2.0A resolution showed that beta4Gal-T1 is in a closed conformation with the oligosaccharide bound to the enzyme, and the 1,2-1,6-arm trisaccharide makes the maximum number of interactions with the enzyme, which is in concurrence with the lowest K(m) for the trisaccharide. Present studies suggest that beta4Gal-T1 interacts preferentially with the 1,2-1,6-arm trisaccharide rather than with the 1,2-1,3-arm or 1,4-1,3-arm of a bi- or tri-antennary oligosaccharide chain of N-glycan.

	~~==Function==~~		Oligosaccharide preferences of beta1,4-galactosyltransferase-I: crystal structures of Met340His mutant of human beta1,4-galactosyltransferase-I with a pentasaccharide and trisaccharides of the N-glycan moiety.,Ramasamy V, Ramakrishnan B, Boeggeman E, Ratner DM, Seeberger PH, Qasba PK J Mol Biol. 2005 Oct 14;353(1):53-67. PMID:16157350<ref>PMID:16157350</ref>
	~~[[http~~:~~//www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] The Golgi complex form catalyzes the production~~ of ~~lactose in the lactating mammary gland~~ and ~~could also be responsible for~~ the ~~synthesis of complex-type~~ N-~~linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids~~. ~~The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions~~, ~~as those occurring during development and egg fertilization~~, ~~by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix~~.

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[2aec]] is~~ a ~~3 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:/~~/~~oca.weizmann.ac.il/oca-bin/ocashort?id=2AEC OCA].~~		</div>

	==See Also==		==See Also==
	*[[~~Galactosyltransferase~~\|~~Galactosyltransferase~~]]		*[[Glycosyltransferase\|Glycosyltransferase]]
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:016157350</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: N-acetyllactosamine synthase]]		[[Category: N-acetyllactosamine synthase]]

OCA at 22:47, 24 March 2013

2013-03-24T22:47:22Z

← Older revision		Revision as of 22:47, 24 March 2013
Line 1:		Line 1:
	~~[[Image:2aec.png\|left\|200px]]~~

	{{STRUCTURE_2aec\| PDB=2aec \| SCENE= }}		{{STRUCTURE_2aec\| PDB=2aec \| SCENE= }}
			===Crystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4GAL-T1) in Complex with GlcNAc-beta1,2-Man-alpha1,6-Man-beta-OR===
			{{ABSTRACT_PUBMED_16157350}}

	===~~Crystal Structure~~ of ~~Human M340H-Beta1,4-Galactosyltransferase-I~~ (~~M340H~~-~~B4GAL~~-~~T1) in Complex~~ with ~~GlcNAc~~-~~beta1~~,~~2-Man-alpha1~~,~~6-Man-beta-OR===~~		==Disease==
			[[http://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] Defects in B4GALT1 are the cause of congenital disorder of glycosylation type 2D (CDG2D) [MIM:[http://omim.org/entry/607091 607091]]. CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.

	~~{{ABSTRACT_PUBMED_16157350}}~~		==Function==
			[[http://www.uniprot.org/uniprot/B4GT1_HUMAN B4GT1_HUMAN]] The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.

	==About this Structure==		==About this Structure==
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	==Reference==		==Reference==
	<ref group="xtra">PMID:016157350</ref><references group="xtra"/>		<ref group="xtra">PMID:016157350</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: N-acetyllactosamine synthase]]		[[Category: N-acetyllactosamine synthase]]