3kl0 - Revision history

OCA at 14:05, 13 March 2024

2024-03-13T14:05:34Z

← Older revision		Revision as of 14:05, 13 March 2024
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	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/XYNC_BACSU XYNC_BACSU] Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).<ref>PMID:17028274</ref>		[https://www.uniprot.org/uniprot/XYNC_BACSU XYNC_BACSU] Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).<ref>PMID:17028274</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Xylanases of glycosyl hydrolase family 30 (GH30) have been shown to cleave beta-1,4 linkages of 4-O-methylglucuronoxylan (MeGX(n)) as directed by the position along the xylan chain of an alpha-1,2-linked 4-O-methylglucuronate (MeGA) moiety. Complete hydrolysis of MeGX(n) by these enzymes results in singly substituted aldouronates having a 4-O-methylglucuronate moiety linked to a xylose penultimate from the reducing terminal xylose and some number of xylose residues toward the nonreducing terminus. This novel mode of action distinguishes GH30 xylanases from the more common xylanase families that cleave MeGX(n) in accessible regions. To help understand this unique biochemical function, we have determined the structure of XynC in its native and ligand-bound forms. XynC structure models derived from diffraction data of XynC crystal soaks with the simple sugar glucuronate (GA) and the tetrameric sugar 4-O-methyl-aldotetrauronate resulted in models containing GA and 4-O-methyl-aldotriuronate, respectively. Each is observed in two locations within XynC surface openings. Ligand coordination occurs within the XynC catalytic substrate binding cleft and on the structurally fused side beta-domain demonstrating a substrate targeting role for this putative carbohydrate binding module. Structural data reveal that GA acts as a primary functional appendage for recognition and hydrolysis of the MeGX(n) polymer by the protein. This work compares the structure of XynC with a previously reported homologous enzyme, XynA, from Erwinia chrysanthemi and analyzes the ligand binding sites. Our results identify the molecular interactions that define the unique function of XynC and homologous GH30 enzymes.

	Ligand-Bound Structures of a Glycosyl Hydrolase Family 30 Glucuronoxylan Xylanohydrolase.,St John FJ, Hurlbert JC, Rice JD, Preston JF, Pozharski E J Mol Biol. 2011 Jan 19. PMID:21256135<ref>PMID:21256135</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 3kl0" style="background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:18, 6 September 2023

2023-09-06T08:18:03Z

← Older revision		Revision as of 08:18, 6 September 2023
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	<StructureSection load='3kl0' size='340' side='right'caption='[[3kl0]], [[Resolution\|resolution]] 1.64Å' scene=''>		<StructureSection load='3kl0' size='340' side='right'caption='[[3kl0]], [[Resolution\|resolution]] 1.64Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3kl0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Bacsu Bacsu~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KL0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3kl0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KL0 FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>~~, ~~<scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</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]] 1.64Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[3kl3\|3kl3]], [[3kl5\|3kl5]]~~</~~div~~><~~/td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr>
	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">BSU18150~~, ~~xynC, ynfF ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])~~<~~/td></tr>~~
	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/Glucuronoarabinoxylan_endo~~-~~1,4~~-~~beta-xylanase Glucuronoarabinoxylan endo-1,4-beta-xylanase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.136 3.2.1.136]~~ </~~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=3kl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl0 OCA], [https://pdbe.org/3kl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kl0 RCSB], [https://www.ebi.ac.uk/pdbsum/3kl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kl0 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=3kl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl0 OCA], [https://pdbe.org/3kl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kl0 RCSB], [https://www.ebi.ac.uk/pdbsum/3kl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kl0 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/XYNC_BACSU XYNC_BACSU]] Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).<ref>PMID:17028274</ref>		[https://www.uniprot.org/uniprot/XYNC_BACSU XYNC_BACSU] Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).<ref>PMID:17028274</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: ~~Bacsu]]~~		[[Category: Bacillus subtilis subsp. subtilis str. 168]]
	~~[[Category: Glucuronoarabinoxylan endo-1,4-beta-xylanase~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Hurlbert~~, J C]]~~		[[Category: Hurlbert JC]]
	~~[[Category: John, F J.St~~]]		[[Category: Pozharski E]]
	[[Category: Pozharski, E]]		[[Category: St John FJ]]
	[[Category: ~~Alpha beta barrel]]~~
	~~[[Category: Hydrolase~~]]

OCA at 13:35, 4 May 2022

2022-05-04T13:35:35Z

← Older revision		Revision as of 13:35, 4 May 2022
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	==Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis==		==Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis==
	<StructureSection load='3kl0' size='340' side='right' caption='[[3kl0]], [[Resolution\|resolution]] 1.64Å' scene=''>		<StructureSection load='3kl0' size='340' side='right'caption='[[3kl0]], [[Resolution\|resolution]] 1.64Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3kl0]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KL0 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3KL0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3kl0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KL0 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3kl3\|3kl3]], [[3kl5\|3kl5]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3kl3\|3kl3]], [[3kl5\|3kl5]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BSU18150, xynC, ynfF ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BSU18150, xynC, ynfF ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Glucuronoarabinoxylan_endo-1,4-beta-xylanase Glucuronoarabinoxylan endo-1,4-beta-xylanase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.136 3.2.1.136] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucuronoarabinoxylan_endo-1,4-beta-xylanase Glucuronoarabinoxylan endo-1,4-beta-xylanase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.136 3.2.1.136] </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=3kl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl0 OCA], [~~http~~://pdbe.org/3kl0 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3kl0 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3kl0 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3kl0 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=3kl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl0 OCA], [https://pdbe.org/3kl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kl0 RCSB], [https://www.ebi.ac.uk/pdbsum/3kl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kl0 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/XYNC_BACSU XYNC_BACSU]] Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).<ref>PMID:17028274</ref>		[[https://www.uniprot.org/uniprot/XYNC_BACSU XYNC_BACSU]] Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).<ref>PMID:17028274</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 27:
	[[Category: Bacsu]]		[[Category: Bacsu]]
	[[Category: Glucuronoarabinoxylan endo-1,4-beta-xylanase]]		[[Category: Glucuronoarabinoxylan endo-1,4-beta-xylanase]]
			[[Category: Large Structures]]
	[[Category: Hurlbert, J C]]		[[Category: Hurlbert, J C]]
	[[Category: John, F J.St]]		[[Category: John, F J.St]]

OCA at 18:50, 1 February 2017

2017-02-01T18:50:28Z

← Older revision		Revision as of 18:50, 1 February 2017
Line 1:		Line 1:

	==Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis==		==Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis==
	<StructureSection load='3kl0' size='340' side='right' caption='[[3kl0]], [[Resolution\|resolution]] 1.64Å' scene=''>		<StructureSection load='3kl0' size='340' side='right' caption='[[3kl0]], [[Resolution\|resolution]] 1.64Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BSU18150, xynC, ynfF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BSU18150, xynC, ynfF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucuronoarabinoxylan_endo-1,4-beta-xylanase Glucuronoarabinoxylan endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.136 3.2.1.136] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucuronoarabinoxylan_endo-1,4-beta-xylanase Glucuronoarabinoxylan endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.136 3.2.1.136] </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=3kl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kl0 RCSB], [http://www.ebi.ac.uk/pdbsum/3kl0 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=3kl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl0 OCA], [http://pdbe.org/3kl0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kl0 RCSB], [http://www.ebi.ac.uk/pdbsum/3kl0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kl0 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 3kl0" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 05:45, 30 April 2015

2015-04-30T05:45:37Z

← Older revision		Revision as of 05:45, 30 April 2015
Line 2:		Line 2:
	<StructureSection load='3kl0' size='340' side='right' caption='[[3kl0]], [[Resolution\|resolution]] 1.64Å' scene=''>		<StructureSection load='3kl0' size='340' side='right' caption='[[3kl0]], [[Resolution\|resolution]] 1.64Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3kl0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bacillus_subtilis Bacillus subtilis~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KL0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KL0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3kl0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KL0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KL0 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3kl3\|3kl3]], [[3kl5\|3kl5]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3kl3\|3kl3]], [[3kl5\|3kl5]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BSU18150, xynC, ynfF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~1423 Bacillus subtilis~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BSU18150, xynC, ynfF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucuronoarabinoxylan_endo-1,4-beta-xylanase Glucuronoarabinoxylan endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.136 3.2.1.136] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucuronoarabinoxylan_endo-1,4-beta-xylanase Glucuronoarabinoxylan endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.136 3.2.1.136] </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=3kl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kl0 RCSB], [http://www.ebi.ac.uk/pdbsum/3kl0 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=3kl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kl0 RCSB], [http://www.ebi.ac.uk/pdbsum/3kl0 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/~~XYNC1_BACSU XYNC1_BACSU~~]] Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).<ref>PMID:17028274</ref>		[[http://www.uniprot.org/uniprot/XYNC_BACSU XYNC_BACSU]] Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).<ref>PMID:17028274</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bacillus subtilis~~]]		[[Category: Bacsu]]
	[[Category: Glucuronoarabinoxylan endo-1,4-beta-xylanase]]		[[Category: Glucuronoarabinoxylan endo-1,4-beta-xylanase]]
	[[Category: Hurlbert, J C]]		[[Category: Hurlbert, J C]]

OCA at 14:20, 25 December 2014

2014-12-25T14:20:52Z

← Older revision		Revision as of 14:20, 25 December 2014
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	<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=3kl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kl0 RCSB], [http://www.ebi.ac.uk/pdbsum/3kl0 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=3kl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kl0 RCSB], [http://www.ebi.ac.uk/pdbsum/3kl0 PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/XYNC1_BACSU XYNC1_BACSU]] Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).<ref>PMID:17028274</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 16:54, 18 December 2014

2014-12-18T16:54:32Z

← Older revision		Revision as of 16:54, 18 December 2014
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	~~{{STRUCTURE_3kl0\| PDB~~=3kl0 \| ~~SCENE~~= }}		==Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis==
	===~~Crystal~~ structure of the ~~glucuronoxylan xylanohydrolase XynC from~~ Bacillus subtilis===		<StructureSection load='3kl0' size='340' side='right' caption='[[3kl0]], [[Resolution\|resolution]] 1.64Å' scene=''>
	~~{{ABSTRACT_PUBMED_21256135}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[3kl0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KL0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KL0 FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3kl3\|3kl3]], [[3kl5\|3kl5]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BSU18150, xynC, ynfF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucuronoarabinoxylan_endo-1,4-beta-xylanase Glucuronoarabinoxylan endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.136 3.2.1.136] </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=3kl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kl0 RCSB], [http://www.ebi.ac.uk/pdbsum/3kl0 PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Xylanases of glycosyl hydrolase family 30 (GH30) have been shown to cleave beta-1,4 linkages of 4-O-methylglucuronoxylan (MeGX(n)) as directed by the position along the xylan chain of an alpha-1,2-linked 4-O-methylglucuronate (MeGA) moiety. Complete hydrolysis of MeGX(n) by these enzymes results in singly substituted aldouronates having a 4-O-methylglucuronate moiety linked to a xylose penultimate from the reducing terminal xylose and some number of xylose residues toward the nonreducing terminus. This novel mode of action distinguishes GH30 xylanases from the more common xylanase families that cleave MeGX(n) in accessible regions. To help understand this unique biochemical function, we have determined the structure of XynC in its native and ligand-bound forms. XynC structure models derived from diffraction data of XynC crystal soaks with the simple sugar glucuronate (GA) and the tetrameric sugar 4-O-methyl-aldotetrauronate resulted in models containing GA and 4-O-methyl-aldotriuronate, respectively. Each is observed in two locations within XynC surface openings. Ligand coordination occurs within the XynC catalytic substrate binding cleft and on the structurally fused side beta-domain demonstrating a substrate targeting role for this putative carbohydrate binding module. Structural data reveal that GA acts as a primary functional appendage for recognition and hydrolysis of the MeGX(n) polymer by the protein. This work compares the structure of XynC with a previously reported homologous enzyme, XynA, from Erwinia chrysanthemi and analyzes the ligand binding sites. Our results identify the molecular interactions that define the unique function of XynC and homologous GH30 enzymes.

	~~==Function==~~		Ligand-Bound Structures of a Glycosyl Hydrolase Family 30 Glucuronoxylan Xylanohydrolase.,St John FJ, Hurlbert JC, Rice JD, Preston JF, Pozharski E J Mol Biol. 2011 Jan 19. PMID:21256135<ref>PMID:21256135</ref>
	~~[[http://www.uniprot.org/uniprot/XYNC1_BACSU XYNC1_BACSU]] Catalyzes the depolymerization~~ of ~~methylglucuronoxylan (MeGAXn) from different sources~~. ~~It cleaves the beta-1~~,~~4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1~~,~~2-linked 4-O-methyl-D-glucuronate (MeGA)~~.<ref>PMID:~~17028274~~</ref>

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[3kl0]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bacillus_subtilis Bacillus subtilis]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3KL0 OCA].~~		</div>
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:021256135</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	[[Category: Glucuronoarabinoxylan endo-1,4-beta-xylanase]]		[[Category: Glucuronoarabinoxylan endo-1,4-beta-xylanase]]
	[[Category: Hurlbert, J C.]]		[[Category: Hurlbert, J C]]
	[[Category: John, F J.St.]]		[[Category: John, F J.St]]
	[[Category: Pozharski, E.]]		[[Category: Pozharski, E]]
	[[Category: Alpha beta barrel]]		[[Category: Alpha beta barrel]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 02:41, 4 April 2013

2013-04-04T02:41:39Z

← Older revision		Revision as of 02:41, 4 April 2013
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	~~[[Image:3kl0.png\|left\|200px]]~~

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_3kl0", 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_3kl0\| PDB=3kl0 \| SCENE= }}		{{STRUCTURE_3kl0\| PDB=3kl0 \| SCENE= }}

	===Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis===		===Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis===
			{{ABSTRACT_PUBMED_21256135}}

			==Function==
	~~<!--~~		[[http://www.uniprot.org/uniprot/XYNC1_BACSU XYNC1_BACSU]] Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).<ref>PMID:17028274</ref>
	~~The line below this paragraph, {{ABSTRACT_PUBMED_21256135}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov~~), ~~where 21256135 is~~ the ~~PubMed ID number.~~
	-->
	~~{{ABSTRACT_PUBMED_21256135}}~~

	==About this Structure==		==About this Structure==
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	==Reference==		==Reference==
	<ref group="xtra">PMID:~~21256135~~</ref><references group="xtra"/>		<ref group="xtra">PMID:021256135</ref><references group="xtra"/><references/>
	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	[[Category: Glucuronoarabinoxylan endo-1,4-beta-xylanase]]		[[Category: Glucuronoarabinoxylan endo-1,4-beta-xylanase]]
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	[[Category: John, F J.St.]]		[[Category: John, F J.St.]]
	[[Category: Pozharski, E.]]		[[Category: Pozharski, E.]]
			[[Category: Alpha beta barrel]]
			[[Category: Hydrolase]]

OCA: Protected "3kl0" [edit=sysop:move=sysop]

2011-02-02T05:52:52Z

Protected "3kl0" [edit=sysop:move=sysop]

← Older revision	Revision as of 05:52, 2 February 2011
(No difference)

OCA at 05:52, 2 February 2011

2011-02-02T05:52:50Z

← Older revision		Revision as of 05:52, 2 February 2011
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	~~{{Seed}}~~		[[Image:3kl0.png\|left\|200px]]
	[[Image:3kl0.~~jpg~~\|left\|200px]]

	<!--		<!--
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	===Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis===		===Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis===


			<!--
			The line below this paragraph, {{ABSTRACT_PUBMED_21256135}}, adds the Publication Abstract to the page
			(as it appears on PubMed at http://www.pubmed.gov), where 21256135 is the PubMed ID number.
			-->
			{{ABSTRACT_PUBMED_21256135}}

	==About this Structure==		==About this Structure==
	~~3KL0~~ is a 4 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KL0 OCA].		[[3kl0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KL0 OCA].

			==Reference==
			<ref group="xtra">PMID:21256135</ref><references group="xtra"/>
	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	[[Category: Glucuronoarabinoxylan endo-1,4-beta-xylanase]]		[[Category: Glucuronoarabinoxylan endo-1,4-beta-xylanase]]
Line 20:		Line 28:
	[[Category: John, F J.St.]]		[[Category: John, F J.St.]]
	[[Category: Pozharski, E.]]		[[Category: Pozharski, E.]]
	~~[[Category: Alpha beta barrel]]~~
	~~[[Category: Hydrolase]]~~

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 8 11:47:46 2010''~~