1o7a - Revision history

OCA at 08:55, 10 April 2024

2024-04-10T08:55:36Z

← Older revision		Revision as of 08:55, 10 April 2024
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	<StructureSection load='1o7a' size='340' side='right'caption='[[1o7a]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1o7a' size='340' side='right'caption='[[1o7a]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1o7a]] is a 6 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=1O7A OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1O7A FirstGlance]. <br>		<table><tr><td colspan='2'>[[1o7a]] is a 6 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=1O7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O7A FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</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]] 2.25Å</td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qbd\|1qbd]]</td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </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=1o7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7a OCA], [https://pdbe.org/1o7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o7a RCSB], [https://www.ebi.ac.uk/pdbsum/1o7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7a ProSAT]</span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1o7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7a OCA], [~~http~~://pdbe.org/1o7a PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1o7a RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1o7a PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7a ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[~~[http~~://www.uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN]] Defects in HEXB are the cause of GM2-gangliosidosis type 2 (GM2G2) [MIM:[~~http~~://omim.org/entry/268800 268800]]; also known as Sandhoff disease. GM2-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. GM2G2 is clinically indistinguishable from GM2-gangliosidosis type 1, presenting startle reactions, early blindness, progressive motor and mental deterioration, macrocephaly and cherry-red spots on the macula.<ref>PMID:1720305</ref> <ref>PMID:1531140</ref> <ref>PMID:8357844</ref> <ref>PMID:7626071</ref> <ref>PMID:7557963</ref> <ref>PMID:7633435</ref> <ref>PMID:8950198</ref> <ref>PMID:9401004</ref> <ref>PMID:9856491</ref> <ref>PMID:9694901</ref>		[https://www.uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN] Defects in HEXB are the cause of GM2-gangliosidosis type 2 (GM2G2) [MIM:[https://omim.org/entry/268800 268800]; also known as Sandhoff disease. GM2-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. GM2G2 is clinically indistinguishable from GM2-gangliosidosis type 1, presenting startle reactions, early blindness, progressive motor and mental deterioration, macrocephaly and cherry-red spots on the macula.<ref>PMID:1720305</ref> <ref>PMID:1531140</ref> <ref>PMID:8357844</ref> <ref>PMID:7626071</ref> <ref>PMID:7557963</ref> <ref>PMID:7633435</ref> <ref>PMID:8950198</ref> <ref>PMID:9401004</ref> <ref>PMID:9856491</ref> <ref>PMID:9694901</ref>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN]] Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues.		[https://www.uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN] Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1o7a 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=1o7a ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Human lysosomal beta-hexosaminidases are dimeric enzymes composed of alpha and beta-chains, encoded by the genes HEXA and HEXB. They occur in three isoforms, the homodimeric hexosaminidases B (betabeta) and S (alphaalpha), and the heterodimeric hexosaminidase A (alphabeta), where dimerization is required for catalytic activity. Allelic variations in the HEXA and HEXB genes cause the fatal inborn errors of metabolism Tay-Sachs disease and Sandhoff disease, respectively. Here, we present the crystal structure of a complex of human beta-hexosaminidase B with a transition state analogue inhibitor at 2.3A resolution (pdb 1o7a). On the basis of this structure and previous studies on related enzymes, a retaining double-displacement mechanism for glycosyl hydrolysis by beta-hexosaminidase B is proposed. In the dimer structure, which is derived from an analysis of crystal packing, most of the mutations causing late-onset Sandhoff disease reside near the dimer interface and are proposed to interfere with correct dimer formation. The structure reported here is a valid template also for the dimeric structures of beta-hexosaminidase A and S.

	The X-ray crystal structure of human beta-hexosaminidase B provides new insights into Sandhoff disease.,Maier T, Strater N, Schuette CG, Klingenstein R, Sandhoff K, Saenger W J Mol Biol. 2003 May 2;328(3):669-81. PMID:12706724<ref>PMID:12706724</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 1o7a" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Beta-Hexosaminidase\|Beta-Hexosaminidase]]		*[[Beta-Hexosaminidase\|Beta-Hexosaminidase]]
	*[[Beta-Hexosaminidase 3D structures\|Beta-Hexosaminidase 3D structures]]		*[[Beta-Hexosaminidase 3D structures\|Beta-Hexosaminidase 3D structures]]
			*[[Beta-N-acetylhexosaminidase 3D structures\|Beta-N-acetylhexosaminidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Beta-N-acetylhexosaminidase]]~~		[[Category: Homo sapiens]]
	~~[[Category: Human~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Klingenstein, R]]		[[Category: Klingenstein R]]
	[[Category: Maier, T]]		[[Category: Maier T]]
	[[Category: Saenger, W]]		[[Category: Saenger W]]
	[[Category: Sandhoff, K]]		[[Category: Sandhoff K]]
	[[Category: Schuette, C]]		[[Category: Schuette C]]
	[[Category: Strater, N]]		[[Category: Strater N]]
	~~[[Category: Ba8-barrel]]~~
	~~[[Category: Glycosidase]]~~
	~~[[Category: Glycosyl hydrolase]]~~
	~~[[Category: Hexosaminidase]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Lysosomal]]~~
	~~[[Category: Sandhoff disease]]~~
	~~[[Category: Sphingolipid degradation~~]]

OCA at 09:42, 18 November 2020

2020-11-18T09:42:34Z

← Older revision		Revision as of 09:42, 18 November 2020
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	<StructureSection load='1o7a' size='340' side='right'caption='[[1o7a]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1o7a' size='340' side='right'caption='[[1o7a]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1o7a]] is a 6 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=1O7A OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1O7A FirstGlance]. <br>		<table><tr><td colspan='2'>[[1o7a]] is a 6 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=1O7A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1O7A FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</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" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</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">[[1qbd\|1qbd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qbd\|1qbd]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </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=1o7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7a OCA], [http://pdbe.org/1o7a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7a RCSB], [http://www.ebi.ac.uk/pdbsum/1o7a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7a ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1o7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7a OCA], [http://pdbe.org/1o7a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7a RCSB], [http://www.ebi.ac.uk/pdbsum/1o7a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7a ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 07:17, 24 April 2019

2019-04-24T07:17:14Z

← Older revision		Revision as of 07:17, 24 April 2019
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	==Human beta-Hexosaminidase B==		==Human beta-Hexosaminidase B==
	<StructureSection load='1o7a' size='340' side='right' caption='[[1o7a]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1o7a' size='340' side='right'caption='[[1o7a]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1o7a]] is a 6 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=1O7A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7A FirstGlance]. <br>		<table><tr><td colspan='2'>[[1o7a]] is a 6 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=1O7A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7A FirstGlance]. <br>
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	</div>		</div>
	<div class="pdbe-citations 1o7a" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1o7a" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Beta-Hexosaminidase\|Beta-Hexosaminidase]]
			*[[Beta-Hexosaminidase 3D structures\|Beta-Hexosaminidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Beta-N-acetylhexosaminidase]]		[[Category: Beta-N-acetylhexosaminidase]]
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Klingenstein, R]]		[[Category: Klingenstein, R]]
	[[Category: Maier, T]]		[[Category: Maier, T]]

OCA at 07:34, 7 February 2018

2018-02-07T07:34:20Z

← Older revision		Revision as of 07:34, 7 February 2018
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	==Human beta-Hexosaminidase B==		==Human beta-Hexosaminidase B==
	<StructureSection load='1o7a' size='340' side='right' caption='[[1o7a]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1o7a' size='340' side='right' caption='[[1o7a]], [[Resolution\|resolution]] 2.25Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qbd\|1qbd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qbd\|1qbd]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </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=1o7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7a OCA], [http://pdbe.org/1o7a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7a RCSB], [http://www.ebi.ac.uk/pdbsum/1o7a 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=1o7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7a OCA], [http://pdbe.org/1o7a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7a RCSB], [http://www.ebi.ac.uk/pdbsum/1o7a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7a ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/1o7a_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/1o7a_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>
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	</div>		</div>
	<div class="pdbe-citations 1o7a" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1o7a" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Beta-Hexosaminidase\|Beta-Hexosaminidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:45, 7 February 2016

2016-02-07T09:45:22Z

← Older revision		Revision as of 09:45, 7 February 2016
Line 20:		Line 20:
	<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=1o7a ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 00:14, 10 September 2015

2015-09-10T00:14:25Z

← Older revision		Revision as of 00:14, 10 September 2015
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	<StructureSection load='1o7a' size='340' side='right' caption='[[1o7a]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1o7a' size='340' side='right' caption='[[1o7a]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1o7a]] is a 6 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=1O7A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7A FirstGlance]. <br>		<table><tr><td colspan='2'>[[1o7a]] is a 6 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=1O7A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7A FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</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">[[1qbd\|1qbd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qbd\|1qbd]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </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=1o7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o7a RCSB], [http://www.ebi.ac.uk/pdbsum/1o7a 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=1o7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7a OCA], [http://pdbe.org/1o7a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7a RCSB], [http://www.ebi.ac.uk/pdbsum/1o7a PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 30:		Line 30:
	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 1o7a" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Beta-N-acetylhexosaminidase]]		[[Category: Beta-N-acetylhexosaminidase]]
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Klingenstein, R]]		[[Category: Klingenstein, R]]
	[[Category: Maier, T]]		[[Category: Maier, T]]

OCA at 17:05, 5 January 2015

2015-01-05T17:05:38Z

← Older revision		Revision as of 17:05, 5 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1o7a]] is a 6 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=1O7A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7A FirstGlance]. <br>		<table><tr><td colspan='2'>[[1o7a]] is a 6 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=1O7A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7A FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</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">[[1qbd\|1qbd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qbd\|1qbd]]</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </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=1o7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o7a RCSB], [http://www.ebi.ac.uk/pdbsum/1o7a 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=1o7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o7a RCSB], [http://www.ebi.ac.uk/pdbsum/1o7a PDBsum]</span></td></tr>
	<table>		</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN]] Defects in HEXB are the cause of GM2-gangliosidosis type 2 (GM2G2) [MIM:[http://omim.org/entry/268800 268800]]; also known as Sandhoff disease. GM2-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. GM2G2 is clinically indistinguishable from GM2-gangliosidosis type 1, presenting startle reactions, early blindness, progressive motor and mental deterioration, macrocephaly and cherry-red spots on the macula.<ref>PMID:1720305</ref> <ref>PMID:1531140</ref> <ref>PMID:8357844</ref> <ref>PMID:7626071</ref> <ref>PMID:7557963</ref> <ref>PMID:7633435</ref> <ref>PMID:8950198</ref> <ref>PMID:9401004</ref> <ref>PMID:9856491</ref> <ref>PMID:9694901</ref>		[[http://www.uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN]] Defects in HEXB are the cause of GM2-gangliosidosis type 2 (GM2G2) [MIM:[http://omim.org/entry/268800 268800]]; also known as Sandhoff disease. GM2-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. GM2G2 is clinically indistinguishable from GM2-gangliosidosis type 1, presenting startle reactions, early blindness, progressive motor and mental deterioration, macrocephaly and cherry-red spots on the macula.<ref>PMID:1720305</ref> <ref>PMID:1531140</ref> <ref>PMID:8357844</ref> <ref>PMID:7626071</ref> <ref>PMID:7557963</ref> <ref>PMID:7633435</ref> <ref>PMID:8950198</ref> <ref>PMID:9401004</ref> <ref>PMID:9856491</ref> <ref>PMID:9694901</ref>
Line 39:		Line 39:
	[[Category: Beta-N-acetylhexosaminidase]]		[[Category: Beta-N-acetylhexosaminidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Klingenstein, R.]]		[[Category: Klingenstein, R]]
	[[Category: Maier, T.]]		[[Category: Maier, T]]
	[[Category: Saenger, W.]]		[[Category: Saenger, W]]
	[[Category: Sandhoff, K.]]		[[Category: Sandhoff, K]]
	[[Category: Schuette, C.]]		[[Category: Schuette, C]]
	[[Category: Strater, N.]]		[[Category: Strater, N]]
	[[Category: Ba8-barrel]]		[[Category: Ba8-barrel]]
	[[Category: Glycosidase]]		[[Category: Glycosidase]]

OCA at 15:45, 29 September 2014

2014-09-29T15:45:37Z

← Older revision		Revision as of 15:45, 29 September 2014
Line 1:		Line 1:
	~~{{STRUCTURE_1o7a~~\| ~~PDB~~=1o7a \| ~~SCENE~~= }}		==Human beta-Hexosaminidase B==
	===~~Human beta~~-~~Hexosaminidase B~~===		<StructureSection load='1o7a' size='340' side='right' caption='[[1o7a]], [[Resolution\|resolution]] 2.25Å' scene=''>
	~~{{ABSTRACT_PUBMED_12706724}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[1o7a]] is a 6 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=1O7A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7A FirstGlance]. <br>
	==Disease==		</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
	[[http://www.uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN]] Defects in HEXB are the cause of GM2-gangliosidosis type 2 (GM2G2) [MIM:[http://omim.org/entry/268800 268800]]; also known as Sandhoff disease. GM2-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. GM2G2 is clinically indistinguishable from GM2-gangliosidosis type 1, presenting startle reactions, early blindness, progressive motor and mental deterioration, macrocephaly and cherry-red spots on the macula.<ref>PMID:1720305</ref><ref>PMID:1531140</ref><ref>PMID:8357844</ref><ref>PMID:7626071</ref><ref>PMID:7557963</ref><ref>PMID:7633435</ref><ref>PMID:8950198</ref><ref>PMID:9401004</ref><ref>PMID:9856491</ref><ref>PMID:9694901</ref>		<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qbd\|1qbd]]</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </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=1o7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o7a RCSB], [http://www.ebi.ac.uk/pdbsum/1o7a PDBsum]</span></td></tr>
			<table>
			== Disease ==
			[[http://www.uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN]] Defects in HEXB are the cause of GM2-gangliosidosis type 2 (GM2G2) [MIM:[http://omim.org/entry/268800 268800]]; also known as Sandhoff disease. GM2-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. GM2G2 is clinically indistinguishable from GM2-gangliosidosis type 1, presenting startle reactions, early blindness, progressive motor and mental deterioration, macrocephaly and cherry-red spots on the macula.<ref>PMID:1720305</ref> <ref>PMID:1531140</ref> <ref>PMID:8357844</ref> <ref>PMID:7626071</ref> <ref>PMID:7557963</ref> <ref>PMID:7633435</ref> <ref>PMID:8950198</ref> <ref>PMID:9401004</ref> <ref>PMID:9856491</ref> <ref>PMID:9694901</ref>
			== Function ==
			[[http://www.uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN]] Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues.
			== 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/o7/1o7a_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 ==
			Human lysosomal beta-hexosaminidases are dimeric enzymes composed of alpha and beta-chains, encoded by the genes HEXA and HEXB. They occur in three isoforms, the homodimeric hexosaminidases B (betabeta) and S (alphaalpha), and the heterodimeric hexosaminidase A (alphabeta), where dimerization is required for catalytic activity. Allelic variations in the HEXA and HEXB genes cause the fatal inborn errors of metabolism Tay-Sachs disease and Sandhoff disease, respectively. Here, we present the crystal structure of a complex of human beta-hexosaminidase B with a transition state analogue inhibitor at 2.3A resolution (pdb 1o7a). On the basis of this structure and previous studies on related enzymes, a retaining double-displacement mechanism for glycosyl hydrolysis by beta-hexosaminidase B is proposed. In the dimer structure, which is derived from an analysis of crystal packing, most of the mutations causing late-onset Sandhoff disease reside near the dimer interface and are proposed to interfere with correct dimer formation. The structure reported here is a valid template also for the dimeric structures of beta-hexosaminidase A and S.

	~~==Function==~~		The X-ray crystal structure of human beta-hexosaminidase B provides new insights into Sandhoff disease.,Maier T, Strater N, Schuette CG, Klingenstein R, Sandhoff K, Saenger W J Mol Biol. 2003 May 2;328(3):669-81. PMID:12706724<ref>PMID:12706724</ref>
	~~[[http://www~~.~~uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN]] Responsible for the degradation of GM2 gangliosides~~, ~~and a variety of other molecules containing terminal~~ N-~~acetyl hexosamines, in the brain and other tissues~~.

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[1o7a]] is~~ a ~~6 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=1O7A OCA].~~		</div>

	==See Also==		==See Also==
	*[[Beta-Hexosaminidase\|Beta-Hexosaminidase]]		*[[Beta-Hexosaminidase\|Beta-Hexosaminidase]]
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:012706724</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Beta-N-acetylhexosaminidase]]		[[Category: Beta-N-acetylhexosaminidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 17:55, 24 March 2013

2013-03-24T17:55:48Z

← Older revision		Revision as of 17:55, 24 March 2013
Line 1:		Line 1:
	~~[[Image:1o7a.png\|left\|200px]]~~

	{{STRUCTURE_1o7a\| PDB=1o7a \| SCENE= }}		{{STRUCTURE_1o7a\| PDB=1o7a \| SCENE= }}
			===Human beta-Hexosaminidase B===
			{{ABSTRACT_PUBMED_12706724}}

	===~~Human beta~~-~~Hexosaminidase B===~~		==Disease==
			[[http://www.uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN]] Defects in HEXB are the cause of GM2-gangliosidosis type 2 (GM2G2) [MIM:[http://omim.org/entry/268800 268800]]; also known as Sandhoff disease. GM2-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. GM2G2 is clinically indistinguishable from GM2-gangliosidosis type 1, presenting startle reactions, early blindness, progressive motor and mental deterioration, macrocephaly and cherry-red spots on the macula.<ref>PMID:1720305</ref><ref>PMID:1531140</ref><ref>PMID:8357844</ref><ref>PMID:7626071</ref><ref>PMID:7557963</ref><ref>PMID:7633435</ref><ref>PMID:8950198</ref><ref>PMID:9401004</ref><ref>PMID:9856491</ref><ref>PMID:9694901</ref>

	~~{{ABSTRACT_PUBMED_12706724}}~~		==Function==
			[[http://www.uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN]] Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues.

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
	<ref group="xtra">PMID:012706724</ref><references group="xtra"/>		<ref group="xtra">PMID:012706724</ref><references group="xtra"/><references/>
	[[Category: Beta-N-acetylhexosaminidase]]		[[Category: Beta-N-acetylhexosaminidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 06:16, 20 October 2012

2012-10-20T06:16:40Z

← Older revision		Revision as of 06:16, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[1o7a]] is a 6 chain structure ~~of [[Beta-Hexosaminidase]]~~ 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=1O7A OCA].		[[1o7a]] is a 6 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=1O7A OCA].

	==See Also==		==See Also==
Line 14:		Line 14:

	==Reference==		==Reference==
	<ref group="xtra">PMID:012706724~~</ref><ref group="xtra">PMID:011447134</ref><ref group="xtra">PMID:001967020~~</ref><references group="xtra"/>		<ref group="xtra">PMID:012706724</ref><references group="xtra"/>
	[[Category: Beta-N-acetylhexosaminidase]]		[[Category: Beta-N-acetylhexosaminidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]