3thd - Revision history

OCA at 17:32, 1 November 2023

2023-11-01T17:32:21Z

← Older revision		Revision as of 17:32, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3thd' size='340' side='right'caption='[[3thd]], [[Resolution\|resolution]] 1.79Å' scene=''>		<StructureSection load='3thd' size='340' side='right'caption='[[3thd]], [[Resolution\|resolution]] 1.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3thd]] is a 4 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=3THD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3THD FirstGlance]. <br>		<table><tr><td colspan='2'>[[3thd]] is a 4 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=3THD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3THD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGJ:(2R,3S,4R,5S)-2-(HYDROXYMETHYL)PIPERIDINE-3,4,5-TRIOL'>DGJ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.79Å</td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3thc\|3thc]]</div></td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGJ:(2R,3S,4R,5S)-2-(HYDROXYMETHYL)PIPERIDINE-3,4,5-TRIOL'>DGJ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GLB1, ELNR1 ([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/Beta-galactosidase Beta-galactosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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=3thd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thd OCA], [https://pdbe.org/3thd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3thd RCSB], [https://www.ebi.ac.uk/pdbsum/3thd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3thd 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=3thd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thd OCA], [https://pdbe.org/3thd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3thd RCSB], [https://www.ebi.ac.uk/pdbsum/3thd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3thd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[https://omim.org/entry/230500 230500]]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> GM1-gangliosidosis 2 (GM1G2) [MIM:[https://omim.org/entry/230600 230600]]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref> GM1-gangliosidosis 3 (GM1G3) [MIM:[https://omim.org/entry/230650 230650]]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref> Mucopolysaccharidosis 4B (MPS4B) [MIM:[https://omim.org/entry/253010 253010]]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>		[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[https://omim.org/entry/230500 230500]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> GM1-gangliosidosis 2 (GM1G2) [MIM:[https://omim.org/entry/230600 230600]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref> GM1-gangliosidosis 3 (GM1G3) [MIM:[https://omim.org/entry/230650 230650]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref> Mucopolysaccharidosis 4B (MPS4B) [MIM:[https://omim.org/entry/253010 253010]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>		[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Beta-galactosidase]]~~		[[Category: Homo sapiens]]
	~~[[Category: Human~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Ohto, U]]		[[Category: Ohto U]]
	[[Category: Shimizu, T]]		[[Category: Shimizu T]]
	~~[[Category: Glycosyl hydrolase]]~~
	~~[[Category: Glycosylation]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Tim-barrel domain~~]]

OCA at 16:58, 6 July 2022

2022-07-06T16:58:13Z

← Older revision		Revision as of 16:58, 6 July 2022
Line 1:		Line 1:

	==Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin==		==Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin==
	<StructureSection load='3thd' size='340' side='right' caption='[[3thd]], [[Resolution\|resolution]] 1.79Å' scene=''>		<StructureSection load='3thd' size='340' side='right'caption='[[3thd]], [[Resolution\|resolution]] 1.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3thd]] is a 4 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=3THD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3THD FirstGlance]. <br>		<table><tr><td colspan='2'>[[3thd]] is a 4 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=3THD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3THD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGJ:(2R,3S,4R,5S)-2-(HYDROXYMETHYL)PIPERIDINE-3,4,5-TRIOL'>DGJ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGJ:(2R,3S,4R,5S)-2-(HYDROXYMETHYL)PIPERIDINE-3,4,5-TRIOL'>DGJ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3thc\|3thc]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3thc\|3thc]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GLB1, ELNR1 ([~~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">GLB1, ELNR1 ([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'>[~~http~~://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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=3thd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thd OCA], [~~http~~://pdbe.org/3thd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3thd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3thd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3thd 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=3thd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thd OCA], [https://pdbe.org/3thd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3thd RCSB], [https://www.ebi.ac.uk/pdbsum/3thd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3thd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[~~http~~://omim.org/entry/230500 230500]]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> GM1-gangliosidosis 2 (GM1G2) [MIM:[~~http~~://omim.org/entry/230600 230600]]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref> GM1-gangliosidosis 3 (GM1G3) [MIM:[~~http~~://omim.org/entry/230650 230650]]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref> Mucopolysaccharidosis 4B (MPS4B) [MIM:[~~http~~://omim.org/entry/253010 253010]]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>		[[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[https://omim.org/entry/230500 230500]]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> GM1-gangliosidosis 2 (GM1G2) [MIM:[https://omim.org/entry/230600 230600]]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref> GM1-gangliosidosis 3 (GM1G3) [MIM:[https://omim.org/entry/230650 230650]]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref> Mucopolysaccharidosis 4B (MPS4B) [MIM:[https://omim.org/entry/253010 253010]]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>		[[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:

	==See Also==		==See Also==
	*[[Galactosidase\|Galactosidase]]		*[[Galactosidase 3D structures\|Galactosidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 32:		Line 32:
	[[Category: Beta-galactosidase]]		[[Category: Beta-galactosidase]]
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Ohto, U]]		[[Category: Ohto, U]]
	[[Category: Shimizu, T]]		[[Category: Shimizu, T]]

OCA at 19:33, 4 August 2016

2016-08-04T19:33:04Z

← Older revision		Revision as of 19:33, 4 August 2016
Line 1:		Line 1:

	==Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin==		==Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin==
	<StructureSection load='3thd' size='340' side='right' caption='[[3thd]], [[Resolution\|resolution]] 1.79Å' scene=''>		<StructureSection load='3thd' size='340' side='right' caption='[[3thd]], [[Resolution\|resolution]] 1.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3thd]] is a 4 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=3THD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3THD FirstGlance]. <br>		<table><tr><td colspan='2'>[[3thd]] is a 4 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=3THD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3THD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGJ:(2R,3S,4R,5S)-2-(HYDROXYMETHYL)PIPERIDINE-3,4,5-TRIOL'>DGJ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGJ:(2R,3S,4R,5S)-2-(HYDROXYMETHYL)PIPERIDINE-3,4,5-TRIOL'>DGJ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3thc\|3thc]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3thc\|3thc]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GLB1, ELNR1 ([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">GLB1, ELNR1 ([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/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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=3thd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3thd RCSB], [http://www.ebi.ac.uk/pdbsum/3thd 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=3thd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thd OCA], [http://pdbe.org/3thd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3thd RCSB], [http://www.ebi.ac.uk/pdbsum/3thd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3thd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 21:		Line 22:
	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 3thd" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 29:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Beta-galactosidase]]		[[Category: Beta-galactosidase]]
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Ohto, U]]		[[Category: Ohto, U]]
	[[Category: Shimizu, T]]		[[Category: Shimizu, T]]

OCA at 07:06, 21 December 2014

2014-12-21T07:06:57Z

← Older revision		Revision as of 07:06, 21 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_3thd\| PDB=3thd \| SCENE= }}~~		==Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin==
	===Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin===		<StructureSection load='3thd' size='340' side='right' caption='[[3thd]], [[Resolution\|resolution]] 1.79Å' scene=''>
	~~{{ABSTRACT_PUBMED_22128166}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[3thd]] is a 4 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=3THD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3THD FirstGlance]. <br>
	==Disease==		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGJ:(2R,3S,4R,5S)-2-(HYDROXYMETHYL)PIPERIDINE-3,4,5-TRIOL'>DGJ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3thc\|3thc]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GLB1, ELNR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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=3thd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3thd RCSB], [http://www.ebi.ac.uk/pdbsum/3thd PDBsum]</span></td></tr>
			</table>
			== Disease ==
	[[http://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[http://omim.org/entry/230500 230500]]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> GM1-gangliosidosis 2 (GM1G2) [MIM:[http://omim.org/entry/230600 230600]]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref> GM1-gangliosidosis 3 (GM1G3) [MIM:[http://omim.org/entry/230650 230650]]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref> Mucopolysaccharidosis 4B (MPS4B) [MIM:[http://omim.org/entry/253010 253010]]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>		[[http://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[http://omim.org/entry/230500 230500]]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> GM1-gangliosidosis 2 (GM1G2) [MIM:[http://omim.org/entry/230600 230600]]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref> GM1-gangliosidosis 3 (GM1G3) [MIM:[http://omim.org/entry/230650 230650]]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref> Mucopolysaccharidosis 4B (MPS4B) [MIM:[http://omim.org/entry/253010 253010]]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>
			== Function ==
			[[http://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			G(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme beta-d-galactosidase (beta-Gal), which lead to accumulations of the beta-Gal substrates, G(M1) ganglioside, and keratan sulfate. beta-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal beta-linked galactose residues. This study shows the crystal structures of human beta-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human beta-Gal is composed of a catalytic TIM barrel domain followed by beta-domain 1 and beta-domain 2. To gain structural insight into the molecular defects of beta-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed.

	~~==Function==~~		Crystal structure of human beta-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.,Ohto U, Usui K, Ochi T, Yuki K, Satow Y, Shimizu T J Biol Chem. 2012 Jan 13;287(3):1801-12. doi: 10.1074/jbc.M111.293795. Epub 2011 , Nov 28. PMID:22128166<ref>PMID:22128166</ref>
	~~[[http://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves~~ beta-~~linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID~~:~~8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation~~ of ~~extracellular elastic fibers (elastogenesis)~~ and ~~in the development of connective tissue~~. ~~Seems to be identical to the elastin-binding protein (EBP)~~, ~~a major component of the non-integrin cell surface receptor expressed on fibroblasts~~, ~~smooth muscle cells~~, ~~chondroblasts~~, ~~leukocytes~~, ~~and certain cancer cell types~~. ~~In elastin producing cells~~, ~~associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers~~.<ref>PMID:~~8922281~~</ref>

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[3thd]] is~~ a ~~4 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=3THD OCA].~~		</div>

	==See Also==		==See Also==
	*[[Galactosidase\|Galactosidase]]		*[[Galactosidase\|Galactosidase]]
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:022128166</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Beta-galactosidase]]		[[Category: Beta-galactosidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ohto, U.]]		[[Category: Ohto, U]]
	[[Category: Shimizu, T~~.]]~~		[[Category: Shimizu, T]]
	~~[[Category: Beta-galactosidase~~]]
	[[Category: Glycosyl hydrolase]]		[[Category: Glycosyl hydrolase]]
	[[Category: Glycosylation]]		[[Category: Glycosylation]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Tim-barrel domain]]		[[Category: Tim-barrel domain]]

OCA at 14:01, 10 July 2013

2013-07-10T14:01:35Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{STRUCTURE_3thd|  PDB=3thd  |  SCENE=  }}
-The entry 3thd is ON HOLD  until Paper Publication
+==Disease==
-Authors: Ohto, U., Shimizu, T.
+==Function==
-Description: Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin
+==About this Structure==

OCA at 05:14, 28 September 2011

2011-09-28T05:14:37Z

← Older revision		Revision as of 05:14, 28 September 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 3thd is ON HOLD		The entry 3thd is ON HOLD until Paper Publication

	Authors: Ohto, U., Shimizu, T.		Authors: Ohto, U., Shimizu, T.

	Description: Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin		Description: Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin

OCA: Protected "3thd" [edit=sysop:move=sysop]

2011-08-24T07:14:04Z

Protected "3thd" [edit=sysop:move=sysop]

← Older revision	Revision as of 07:14, 24 August 2011
(No difference)

OCA: New page: '''Unreleased structure''' The entry 3thd is ON HOLD Authors: Ohto, U., Shimizu, T. Description: Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin

2011-08-24T07:14:03Z

New page: '''Unreleased structure''' The entry 3thd is ON HOLD Authors: Ohto, U., Shimizu, T. Description: Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin

New page

'''Unreleased structure'''

The entry 3thd is ON HOLD

Authors: Ohto, U., Shimizu, T.

Description: Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin