2zut - Revision history

OCA at 13:58, 13 March 2024

OCA — Wed, 13 Mar 2024 13:58:38 GMT

←Older revision		Revision as of 13:58, 13 March 2024
Line 3:		Line 3:
	<StructureSection load='2zut' size='340' side='right'caption='[[2zut]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2zut' size='340' side='right'caption='[[2zut]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2zut]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~As_1.2186 As 1.2186~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZUT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2zut]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum Bifidobacterium longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZUT FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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]] 1.9Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zus\|2zus]], [[2zuu\|2zuu]], [[2zuv\|2zuv]], [[2zuw\|2zuw]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lnpA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216816 AS 1.2186])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/1,3-beta-galactosyl-N-acetylhexosamine_phosphorylase 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.211 2.4.1.211] </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=2zut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zut OCA], [https://pdbe.org/2zut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zut RCSB], [https://www.ebi.ac.uk/pdbsum/2zut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zut 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=2zut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zut OCA], [https://pdbe.org/2zut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zut RCSB], [https://www.ebi.ac.uk/pdbsum/2zut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zut ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/LNPA_BIFL2 LNPA_BIFL2]] Reversibly phosphorolyzes lacto-N-biose to Gal1-P and N-acetylglucosamine (GlcNAc) and galacto-N-biose to Gal1-P and N-acetylgalactosamine (GalNAc). Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria.<ref>PMID:15933016</ref> <ref>PMID:17720833</ref> <ref>PMID:19124470</ref>	+	[https://www.uniprot.org/uniprot/LNPA_BIFL2 LNPA_BIFL2] Reversibly phosphorolyzes lacto-N-biose to Gal1-P and N-acetylglucosamine (GlcNAc) and galacto-N-biose to Gal1-P and N-acetylgalactosamine (GalNAc). Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria.<ref>PMID:15933016</ref> <ref>PMID:17720833</ref> <ref>PMID:19124470</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 22:		Line 20:
	</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=2zut 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=2zut ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Galacto-N-biose/lacto-N-biose I phosphorylase (GLNBP) from Bifidobacterium longum, a key enzyme for intestinal growth, phosphorolyses galacto-N-biose and lacto-N-biose I with anomeric inversion. GLNBP homologues are often found in human pathogenic and commensal bacteria, and their substrate specificities potentially define the nutritional acquisition ability of these microbes in their habitat. We report the crystal structures of GLNBP in five different ligand-binding forms. This is the first three-dimensional structure of glycoside hydrolase (GH) family 112. The GlcNAc- and GalNAc-bound forms provide structural insights into distinct substrate preferences of GLNBP and its homologues from pathogens. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a thermophilic beta-galactosidase, strongly supporting the current classification of GLNBP homologues as one of the GH families. Anion binding induces a large conformational change by rotating a half-unit of the barrel. This is an unusual example of molecular adaptation of a TIM barrel scaffold to substrates.
-
-	The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: a large deformation of a TIM barrel scaffold.,Hidaka M, Nishimoto M, Kitaoka M, Wakagi T, Shoun H, Fushinobu S J Biol Chem. 2009 Mar 13;284(11):7273-83. Epub 2009 Jan 5. PMID:19124470<ref>PMID:19124470</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2zut" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]~~	+	[[Category: Bifidobacterium longum]]
-	~~[[Category: As 1 2186~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Fushinobu, S]]	+	[[Category: Fushinobu S]]
-	[[Category: Hidaka, M]]	+	[[Category: Hidaka M]]
-	[[Category: Kitaoka, M]]	+	[[Category: Kitaoka M]]
-	[[Category: Nishimoto, M]]	+	[[Category: Nishimoto M]]
-	[[Category: Shoun, H]]	+	[[Category: Shoun H]]
-	[[Category: Wakagi, T]]	+	[[Category: Wakagi T]]
-	~~[[Category: Beta-alpha-barrel]]~~	+
-	~~[[Category: Glycosyltransferase]]~~	+
-	~~[[Category: Tim barrel]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 17:38, 15 December 2021

OCA — Wed, 15 Dec 2021 17:38:34 GMT

←Older revision		Revision as of 17:38, 15 December 2021
Line 1:		Line 1:

	==Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc==		==Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc==
-	<StructureSection load='2zut' size='340' side='right' caption='[[2zut]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='2zut' size='340' side='right'caption='[[2zut]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2zut]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/As_1.2186 As 1.2186]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2ZUT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2zut]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/As_1.2186 As 1.2186]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZUT FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zus\|2zus]], [[2zuu\|2zuu]], [[2zuv\|2zuv]], [[2zuw\|2zuw]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zus\|2zus]], [[2zuu\|2zuu]], [[2zuv\|2zuv]], [[2zuw\|2zuw]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lnpA ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216816 AS 1.2186])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lnpA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216816 AS 1.2186])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/1,3-beta-galactosyl-N-acetylhexosamine_phosphorylase 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.211 2.4.1.211] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/1,3-beta-galactosyl-N-acetylhexosamine_phosphorylase 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.211 2.4.1.211] </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=2zut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zut OCA], [~~http~~://pdbe.org/2zut PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2zut RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2zut PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2zut 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=2zut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zut OCA], [https://pdbe.org/2zut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zut RCSB], [https://www.ebi.ac.uk/pdbsum/2zut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zut ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/LNPA_BIFL2 LNPA_BIFL2]] Reversibly phosphorolyzes lacto-N-biose to Gal1-P and N-acetylglucosamine (GlcNAc) and galacto-N-biose to Gal1-P and N-acetylgalactosamine (GalNAc). Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria.<ref>PMID:15933016</ref> <ref>PMID:17720833</ref> <ref>PMID:19124470</ref>	+	[[https://www.uniprot.org/uniprot/LNPA_BIFL2 LNPA_BIFL2]] Reversibly phosphorolyzes lacto-N-biose to Gal1-P and N-acetylglucosamine (GlcNAc) and galacto-N-biose to Gal1-P and N-acetylgalactosamine (GalNAc). Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria.<ref>PMID:15933016</ref> <ref>PMID:17720833</ref> <ref>PMID:19124470</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zu/2zut_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zu/2zut_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>
Line 37:		Line 37:
	[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]		[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]
	[[Category: As 1 2186]]		[[Category: As 1 2186]]
		+	[[Category: Large Structures]]
	[[Category: Fushinobu, S]]		[[Category: Fushinobu, S]]
	[[Category: Hidaka, M]]		[[Category: Hidaka, M]]

OCA at 14:38, 5 August 2016

OCA — Fri, 05 Aug 2016 14:38:41 GMT

←Older revision		Revision as of 14:38, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc==		==Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc==
	<StructureSection load='2zut' size='340' side='right' caption='[[2zut]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2zut' size='340' side='right' caption='[[2zut]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2zut]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bifidobacterium_longum Bifidobacterium longum~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZUT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2zut]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/As_1.2186 As 1.2186]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZUT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zus\|2zus]], [[2zuu\|2zuu]], [[2zuv\|2zuv]], [[2zuw\|2zuw]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zus\|2zus]], [[2zuu\|2zuu]], [[2zuv\|2zuv]], [[2zuw\|2zuw]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lnpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216816 ~~Bifidobacterium longum~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lnpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216816 AS 1.2186])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,3-beta-galactosyl-N-acetylhexosamine_phosphorylase 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.211 2.4.1.211] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,3-beta-galactosyl-N-acetylhexosamine_phosphorylase 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.211 2.4.1.211] </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=2zut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zut OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zut RCSB], [http://www.ebi.ac.uk/pdbsum/2zut 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=2zut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zut OCA], [http://pdbe.org/2zut PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zut RCSB], [http://www.ebi.ac.uk/pdbsum/2zut PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zut ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~Q5NU17_BIFLO Q5NU17_BIFLO~~]] Reversibly phosphorolyzes lacto-N-biose to Gal1-P and N-acetylglucosamine (GlcNAc) and galacto-N-biose to Gal1-P and N-acetylgalactosamine (GalNAc). Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria.<ref>PMID:15933016</ref> <ref>PMID:17720833</ref> <ref>PMID:19124470</ref>	+	[[http://www.uniprot.org/uniprot/LNPA_BIFL2 LNPA_BIFL2]] Reversibly phosphorolyzes lacto-N-biose to Gal1-P and N-acetylglucosamine (GlcNAc) and galacto-N-biose to Gal1-P and N-acetylgalactosamine (GalNAc). Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria.<ref>PMID:15933016</ref> <ref>PMID:17720833</ref> <ref>PMID:19124470</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		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=2zut ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		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 2zut" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]		[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]
-	[[Category: ~~Bifidobacterium longum~~]]	+	[[Category: As 1 2186]]
	[[Category: Fushinobu, S]]		[[Category: Fushinobu, S]]
	[[Category: Hidaka, M]]		[[Category: Hidaka, M]]

OCA at 19:38, 25 December 2014

OCA — Thu, 25 Dec 2014 19:38:06 GMT

←Older revision		Revision as of 19:38, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2zut]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum Bifidobacterium longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZUT FirstGlance]. <br>		<table><tr><td colspan='2'>[[2zut]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum Bifidobacterium longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZUT FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zus\|2zus]], [[2zuu\|2zuu]], [[2zuv\|2zuv]], [[2zuw\|2zuw]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zus\|2zus]], [[2zuu\|2zuu]], [[2zuv\|2zuv]], [[2zuw\|2zuw]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lnpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216816 Bifidobacterium longum])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lnpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216816 Bifidobacterium longum])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,3-beta-galactosyl-N-acetylhexosamine_phosphorylase 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.211 2.4.1.211] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,3-beta-galactosyl-N-acetylhexosamine_phosphorylase 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.211 2.4.1.211] </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=2zut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zut OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zut RCSB], [http://www.ebi.ac.uk/pdbsum/2zut 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=2zut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zut OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zut RCSB], [http://www.ebi.ac.uk/pdbsum/2zut PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/Q5NU17_BIFLO Q5NU17_BIFLO]] Reversibly phosphorolyzes lacto-N-biose to Gal1-P and N-acetylglucosamine (GlcNAc) and galacto-N-biose to Gal1-P and N-acetylgalactosamine (GalNAc). Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria.<ref>PMID:15933016</ref> <ref>PMID:17720833</ref> <ref>PMID:19124470</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]		[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]
	[[Category: Bifidobacterium longum]]		[[Category: Bifidobacterium longum]]
-	[[Category: Fushinobu, S.]]	+	[[Category: Fushinobu, S]]
-	[[Category: Hidaka, M.]]	+	[[Category: Hidaka, M]]
-	[[Category: Kitaoka, M.]]	+	[[Category: Kitaoka, M]]
-	[[Category: Nishimoto, M.]]	+	[[Category: Nishimoto, M]]
-	[[Category: Shoun, H.]]	+	[[Category: Shoun, H]]
-	[[Category: Wakagi, T.]]	+	[[Category: Wakagi, T]]
	[[Category: Beta-alpha-barrel]]		[[Category: Beta-alpha-barrel]]
	[[Category: Glycosyltransferase]]		[[Category: Glycosyltransferase]]
	[[Category: Tim barrel]]		[[Category: Tim barrel]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 05:23, 2 October 2014

OCA — Thu, 02 Oct 2014 05:23:18 GMT

←Older revision		Revision as of 05:23, 2 October 2014
Line 1:		Line 1:
-	[[~~Image:~~2zut.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc==
		+	<StructureSection load='2zut' size='340' side='right' caption='[[2zut]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2zut]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum Bifidobacterium longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZUT FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zus\|2zus]], [[2zuu\|2zuu]], [[2zuv\|2zuv]], [[2zuw\|2zuw]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lnpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216816 Bifidobacterium longum])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,3-beta-galactosyl-N-acetylhexosamine_phosphorylase 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.211 2.4.1.211] </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=2zut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zut OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zut RCSB], [http://www.ebi.ac.uk/pdbsum/2zut PDBsum]</span></td></tr>
		+	<table>
		+	== 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/zu/2zut_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 ==
		+	Galacto-N-biose/lacto-N-biose I phosphorylase (GLNBP) from Bifidobacterium longum, a key enzyme for intestinal growth, phosphorolyses galacto-N-biose and lacto-N-biose I with anomeric inversion. GLNBP homologues are often found in human pathogenic and commensal bacteria, and their substrate specificities potentially define the nutritional acquisition ability of these microbes in their habitat. We report the crystal structures of GLNBP in five different ligand-binding forms. This is the first three-dimensional structure of glycoside hydrolase (GH) family 112. The GlcNAc- and GalNAc-bound forms provide structural insights into distinct substrate preferences of GLNBP and its homologues from pathogens. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a thermophilic beta-galactosidase, strongly supporting the current classification of GLNBP homologues as one of the GH families. Anion binding induces a large conformational change by rotating a half-unit of the barrel. This is an unusual example of molecular adaptation of a TIM barrel scaffold to substrates.

-	~~{{STRUCTURE_2zut\| PDB=2zut \| SCENE= }}~~	+	The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: a large deformation of a TIM barrel scaffold.,Hidaka M, Nishimoto M, Kitaoka M, Wakagi T, Shoun H, Fushinobu S J Biol Chem. 2009 Mar 13;284(11):7273-83. Epub 2009 Jan 5. PMID:19124470<ref>PMID:19124470</ref>

-	~~===Crystal structure of Galacto-N-biose~~/~~Lacto-N-biose I phosphorylase in complex with GalNAc===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_19124470}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2zut]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bifidobacterium_longum Bifidobacterium longum]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:019124470<~~/~~ref~~><~~ref group="xtra">PMID:015933016</ref><references group="xtra"~~/>	+
	[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]		[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]
	[[Category: Bifidobacterium longum]]		[[Category: Bifidobacterium longum]]

OCA at 13:35, 6 February 2013

OCA — Wed, 06 Feb 2013 13:35:13 GMT

←Older revision		Revision as of 13:35, 6 February 2013
Line 1:		Line 1:
	[[Image:2zut.png\|left\|200px]]		[[Image:2zut.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2zut", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2zut\| PDB=2zut \| SCENE= }}		{{STRUCTURE_2zut\| PDB=2zut \| SCENE= }}

	===Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc===		===Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19124470}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19124470 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_19124470}}		{{ABSTRACT_PUBMED_19124470}}

Line 22:		Line 11:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19124470~~</ref><ref group="xtra">PMID:~~15933016~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019124470</ref><ref group="xtra">PMID:015933016</ref><references group="xtra"/>
	[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]		[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]
	[[Category: Bifidobacterium longum]]		[[Category: Bifidobacterium longum]]

OCA: Protected "2zut" [edit=sysop:move=sysop]

OCA — Mon, 14 Mar 2011 20:02:36 GMT

Protected "2zut" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:02, 14 March 2011

OCA at 20:02, 14 March 2011

OCA — Mon, 14 Mar 2011 20:02:34 GMT

←Older revision		Revision as of 20:02, 14 March 2011
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2zut.png\|left\|200px]]		[[Image:2zut.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~2ZUT~~ is a 4 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Bifidobacterium_longum Bifidobacterium longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA].	+	[[2zut]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum Bifidobacterium longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA].

	==Reference==		==Reference==
Line 36:		Line 35:
	[[Category: Tim barrel]]		[[Category: Tim barrel]]
	[[Category: Transferase]]		[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jan 18 09:10:56 2010''

OCA at 07:10, 18 January 2010

OCA — Mon, 18 Jan 2010 07:10:57 GMT

←Older revision		Revision as of 07:10, 18 January 2010
Line 12:		Line 12:
	===Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc===		===Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_19124470}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 19124470 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_19124470}}

	==About this Structure==		==About this Structure==
Line 17:		Line 23:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:15933016</ref><references group="xtra"/>	+	<ref group="xtra">PMID:19124470</ref><ref group="xtra">PMID:15933016</ref><references group="xtra"/>
	[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]		[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]
	[[Category: Bifidobacterium longum]]		[[Category: Bifidobacterium longum]]
Line 31:		Line 37:
	[[Category: Transferase]]		[[Category: Transferase]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun Mar 22 10~~:28:~~16 2009~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jan 18 09:10:56 2010''

OCA at 08:28, 22 March 2009

OCA — Sun, 22 Mar 2009 08:28:16 GMT

←Older revision		Revision as of 08:28, 22 March 2009
Line 12:		Line 12:
	===Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc===		===Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19124470}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19124470 is the PubMed ID number.
-	-->
-	{{ABSTRACT_PUBMED_19124470}}

	==About this Structure==		==About this Structure==
-	2ZUT is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Bifidobacterium_longum Bifidobacterium longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA].	+	2ZUT is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Bifidobacterium_longum Bifidobacterium longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZUT OCA].

	==Reference==		==Reference==
-	The Crystal Structure of Galacto-N-biose/Lacto-N-biose I Phosphorylase: A LARGE DEFORMATION OF A TIM BARREL SCAFFOLD., Hidaka M, Nishimoto M, Kitaoka M, Wakagi T, Shoun H, Fushinobu S, J Biol Chem. 2009 Mar 13;284(11):7273-83. Epub 2009 Jan 5. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/19124470 19124470]~~	+	<ref group="xtra">PMID:15933016</ref><references group="xtra"/>
-		+
-	Novel putative galactose operon involving lacto-N-biose phosphorylase in Bifidobacterium longum., Kitaoka M, Tian J, Nishimoto M, Appl Environ Microbiol. 2005 Jun;71(6):3158-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15933016 15933016]	+
	[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]		[[Category: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase]]
	[[Category: Bifidobacterium longum]]		[[Category: Bifidobacterium longum]]
-	[[Category: ~~Single protein~~]]	+	[[Category: Fushinobu, S.]]
-	[[Category: ~~Pdbx_ordinal=~~, ~~<PDBx~~:~~audit_author~~.]]	+	[[Category: Hidaka, M.]]
		+	[[Category: Kitaoka, M.]]
		+	[[Category: Nishimoto, M.]]
		+	[[Category: Shoun, H.]]
		+	[[Category: Wakagi, T.]]
	[[Category: Beta-alpha-barrel]]		[[Category: Beta-alpha-barrel]]
	[[Category: Glycosyltransferase]]		[[Category: Glycosyltransferase]]
Line 35:		Line 31:
	[[Category: Transferase]]		[[Category: Transferase]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed~~ Mar ~~18 20~~:11:55 2009''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 22 10:28:16 2009''