4lxh - Revision history

OCA at 12:22, 1 March 2024

OCA — Fri, 01 Mar 2024 12:22:37 GMT

←Older revision		Revision as of 12:22, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4lxh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizorhabdus_wittichii_RW1 Rhizorhabdus wittichii RW1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LXH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4lxh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizorhabdus_wittichii_RW1 Rhizorhabdus wittichii RW1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LXH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C1E:(2Z,4E)-3-CHLORO-2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOIC+ACID'>C1E</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.02Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C1E:(2Z,4E)-3-CHLORO-2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOIC+ACID'>C1E</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lxh OCA], [https://pdbe.org/4lxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lxh RCSB], [https://www.ebi.ac.uk/pdbsum/4lxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lxh 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=4lxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lxh OCA], [https://pdbe.org/4lxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lxh RCSB], [https://www.ebi.ac.uk/pdbsum/4lxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lxh ProSAT]</span></td></tr>
	</table>		</table>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	DxnB2 and BphD are meta-cleavage product (MCP) hydrolases that catalyze C-C bond hydrolysis of the biphenyl metabolite 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA). BphD is a bottleneck in the bacterial degradation of polychlorinated biphenyls (PCBs) by the Bph catabolic pathway due in part to inhibition by 3-Cl HOPDAs. By contrast, DxnB2 from Sphingomonas wittichii RW1 catalyzes the hydrolysis of 3-Cl HOPDAs more efficiently. X-ray crystallographic studies of the catalytically inactive S105A variant of DxnB2 complexed with 3-Cl HOPDA revealed a binding mode in which C1 through C6 of the dienoate are coplanar. The chlorine substituent is accommodated by a hydrophobic pocket that is larger than the homologous site in BphDLB400 from Burkholderia xenovorans LB400. The planar binding mode observed in the crystalline complex was consistent with the hyper- and hypsochromically shifted absorption spectra of 3-Cl and 3,9,11-triCl HOPDA, respectively, bound to S105A in solution. Moreover, ES(red), an intermediate possessing a bathochromically shifted spectrum observed in the turnover of HOPDA, was not detected, suggesting that substrate destabilization was rate-limiting in the turnover of these PCB metabolites. Interestingly, electron density for the first alpha-helix of the lid domain was poorly defined in the dimeric DxnB2 structures, unlike in the tetrameric BphDLB400. Structural comparison of MCP hydrolases identified the NC-loop, connecting the lid to the alpha/beta-hydrolase core domain, as a determinant in the oligomeric state and suggests its involvement in catalysis. Finally, an increased mobility of the DxnB2 lid may contribute to the enzyme's ability to hydrolyze PCB metabolites, highlighting how lid architecture contributes to substrate specificity in alpha/beta-hydrolases.
-
-	The Lid Domain of the MCP Hydrolase DxnB2 Contributes to the Reactivity toward Recalcitrant PCB Metabolites.,Ruzzini AC, Bhowmik S, Yam KC, Ghosh S, Bolin JT, Eltis LD Biochemistry. 2013 Aug 20;52(33):5685-95. doi: 10.1021/bi400774m. Epub 2013 Aug, 9. PMID:23879719<ref>PMID:23879719</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4lxh" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 10:38, 21 December 2022

OCA — Wed, 21 Dec 2022 10:38:45 GMT

←Older revision		Revision as of 10:38, 21 December 2022
Line 1:		Line 1:

	==Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from Sphingomonas wittichii RW1, in complex with 3-Cl HOPDA==		==Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from Sphingomonas wittichii RW1, in complex with 3-Cl HOPDA==
-	<StructureSection load='4lxh' size='340' side='right' caption='[[4lxh]], [[Resolution\|resolution]] 2.02Å' scene=''>	+	<StructureSection load='4lxh' size='340' side='right'caption='[[4lxh]], [[Resolution\|resolution]] 2.02Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4lxh]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Sphww Sphww~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4LXH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4lxh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizorhabdus_wittichii_RW1 Rhizorhabdus wittichii RW1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LXH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C1E:(2Z,4E)-3-CHLORO-2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOIC+ACID'>C1E</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C1E:(2Z,4E)-3-CHLORO-2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOIC+ACID'>C1E</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lxg\|4lxg]], [[4lxi\|4lxi]], [[4lyd\|4lyd]]</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=4lxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lxh OCA], [https://pdbe.org/4lxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lxh RCSB], [https://www.ebi.ac.uk/pdbsum/4lxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lxh ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dxnB2, Swit_3055 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=392499 SPHWW])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2,6-dioxo-6-phenylhexa-3-enoate_hydrolase 2,6-dioxo-6-phenylhexa-3-enoate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.8 3.7.1.8] </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=4lxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lxh OCA], [~~http~~://pdbe.org/4lxh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4lxh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4lxh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4lxh ProSAT]</span></td></tr>	+
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 23:		Line 20:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~2,6-dioxo-6-phenylhexa-3-enoate hydrolase~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Sphww~~]]	+	[[Category: Rhizorhabdus wittichii RW1]]
-	[[Category: Bhowmik, S]]	+	[[Category: Bhowmik S]]
-	[[Category: Bolin~~, J T]]~~	+	[[Category: Bolin JT]]
-	~~[[Category: Alpha/beta hydrolase fold]]~~	+
-	~~[[Category: Carbon-carbon bond hydrolase]]~~	+
-	~~[[Category: Cytosolic]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Rossmann fold~~]]	+

OCA at 17:01, 11 August 2016

OCA — Thu, 11 Aug 2016 17:01:19 GMT

←Older revision		Revision as of 17:01, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from Sphingomonas wittichii RW1, in complex with 3-Cl HOPDA==		==Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from Sphingomonas wittichii RW1, in complex with 3-Cl HOPDA==
	<StructureSection load='4lxh' size='340' side='right' caption='[[4lxh]], [[Resolution\|resolution]] 2.02Å' scene=''>		<StructureSection load='4lxh' size='340' side='right' caption='[[4lxh]], [[Resolution\|resolution]] 2.02Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4lxh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Ochroconis_lascauxensis Ochroconis lascauxensis~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LXH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4lxh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sphww Sphww]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LXH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C1E:(2Z,4E)-3-CHLORO-2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOIC+ACID'>C1E</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C1E:(2Z,4E)-3-CHLORO-2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOIC+ACID'>C1E</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lxg\|4lxg]], [[4lxi\|4lxi]], [[4lyd\|4lyd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lxg\|4lxg]], [[4lxi\|4lxi]], [[4lyd\|4lyd]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dxnB2, Swit_3055 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~994323 Ochroconis lascauxensis~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dxnB2, Swit_3055 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=392499 SPHWW])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2,6-dioxo-6-phenylhexa-3-enoate_hydrolase 2,6-dioxo-6-phenylhexa-3-enoate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.8 3.7.1.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2,6-dioxo-6-phenylhexa-3-enoate_hydrolase 2,6-dioxo-6-phenylhexa-3-enoate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.8 3.7.1.8] </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=4lxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lxh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lxh RCSB], [http://www.ebi.ac.uk/pdbsum/4lxh 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=4lxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lxh OCA], [http://pdbe.org/4lxh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lxh RCSB], [http://www.ebi.ac.uk/pdbsum/4lxh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lxh ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 17:		Line 18:
	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 4lxh" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 22:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase]]		[[Category: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase]]
-	[[Category: ~~Ochroconis lascauxensis~~]]	+	[[Category: Sphww]]
	[[Category: Bhowmik, S]]		[[Category: Bhowmik, S]]
	[[Category: Bolin, J T]]		[[Category: Bolin, J T]]

OCA at 10:58, 25 January 2015

OCA — Sun, 25 Jan 2015 10:58:15 GMT

←Older revision		Revision as of 10:58, 25 January 2015
Line 1:		Line 1:
-	~~{{STRUCTURE_4lxh\| PDB=4lxh \| SCENE= }}~~	+	==Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from Sphingomonas wittichii RW1, in complex with 3-Cl HOPDA==
-	===Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from Sphingomonas wittichii RW1, in complex with 3-Cl HOPDA===	+	<StructureSection load='4lxh' size='340' side='right' caption='[[4lxh]], [[Resolution\|resolution]] 2.02Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23879719}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4lxh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ochroconis_lascauxensis Ochroconis lascauxensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LXH FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C1E:(2Z,4E)-3-CHLORO-2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOIC+ACID'>C1E</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lxg\|4lxg]], [[4lxi\|4lxi]], [[4lyd\|4lyd]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dxnB2, Swit_3055 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=994323 Ochroconis lascauxensis])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2,6-dioxo-6-phenylhexa-3-enoate_hydrolase 2,6-dioxo-6-phenylhexa-3-enoate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.8 3.7.1.8] </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=4lxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lxh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lxh RCSB], [http://www.ebi.ac.uk/pdbsum/4lxh PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	DxnB2 and BphD are meta-cleavage product (MCP) hydrolases that catalyze C-C bond hydrolysis of the biphenyl metabolite 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA). BphD is a bottleneck in the bacterial degradation of polychlorinated biphenyls (PCBs) by the Bph catabolic pathway due in part to inhibition by 3-Cl HOPDAs. By contrast, DxnB2 from Sphingomonas wittichii RW1 catalyzes the hydrolysis of 3-Cl HOPDAs more efficiently. X-ray crystallographic studies of the catalytically inactive S105A variant of DxnB2 complexed with 3-Cl HOPDA revealed a binding mode in which C1 through C6 of the dienoate are coplanar. The chlorine substituent is accommodated by a hydrophobic pocket that is larger than the homologous site in BphDLB400 from Burkholderia xenovorans LB400. The planar binding mode observed in the crystalline complex was consistent with the hyper- and hypsochromically shifted absorption spectra of 3-Cl and 3,9,11-triCl HOPDA, respectively, bound to S105A in solution. Moreover, ES(red), an intermediate possessing a bathochromically shifted spectrum observed in the turnover of HOPDA, was not detected, suggesting that substrate destabilization was rate-limiting in the turnover of these PCB metabolites. Interestingly, electron density for the first alpha-helix of the lid domain was poorly defined in the dimeric DxnB2 structures, unlike in the tetrameric BphDLB400. Structural comparison of MCP hydrolases identified the NC-loop, connecting the lid to the alpha/beta-hydrolase core domain, as a determinant in the oligomeric state and suggests its involvement in catalysis. Finally, an increased mobility of the DxnB2 lid may contribute to the enzyme's ability to hydrolyze PCB metabolites, highlighting how lid architecture contributes to substrate specificity in alpha/beta-hydrolases.

-	~~==About this Structure==~~	+	The Lid Domain of the MCP Hydrolase DxnB2 Contributes to the Reactivity toward Recalcitrant PCB Metabolites.,Ruzzini AC, Bhowmik S, Yam KC, Ghosh S, Bolin JT, Eltis LD Biochemistry. 2013 Aug 20;52(33):5685-95. doi: 10.1021/bi400774m. Epub 2013 Aug, 9. PMID:23879719<ref>PMID:23879719</ref>
-	~~[[4lxh]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Ochroconis_lascauxensis Ochroconis lascauxensis]~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4LXH OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:023879719</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase]]		[[Category: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase]]
	[[Category: Ochroconis lascauxensis]]		[[Category: Ochroconis lascauxensis]]
-	[[Category: Bhowmik, S.]]	+	[[Category: Bhowmik, S]]
-	[[Category: Bolin, J T.]]	+	[[Category: Bolin, J T]]
	[[Category: Alpha/beta hydrolase fold]]		[[Category: Alpha/beta hydrolase fold]]
	[[Category: Carbon-carbon bond hydrolase]]		[[Category: Carbon-carbon bond hydrolase]]

OCA at 04:07, 20 September 2013

OCA — Fri, 20 Sep 2013 04:07:25 GMT

←Older revision		Revision as of 04:07, 20 September 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4lxh\| PDB=4lxh \| SCENE= }}
		+	===Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from Sphingomonas wittichii RW1, in complex with 3-Cl HOPDA===
		+	{{ABSTRACT_PUBMED_23879719}}

-	~~The entry~~ 4lxh is ~~ON HOLD~~	+	==About this Structure==
		+	[[4lxh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ochroconis_lascauxensis Ochroconis lascauxensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXH OCA].

-	~~Authors~~: Bhowmik, S., Bolin, J.T.	+	==Reference==
-		+	<ref group="xtra">PMID:023879719</ref><references group="xtra"/><references/>
-	~~Description~~: ~~Crystal Structure of the S105A mutant of a carbon~~-carbon bond hydrolase~~, DxnB2 from Sphingomonas wittichii RW1, in complex with 3-Cl HOPDA~~	+	[[Category: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase]]
		+	[[Category: Ochroconis lascauxensis]]
		+	[[Category: Bhowmik, S.]]
		+	[[Category: Bolin, J T.]]
		+	[[Category: Alpha/beta hydrolase fold]]
		+	[[Category: Carbon-carbon bond hydrolase]]
		+	[[Category: Cytosolic]]
		+	[[Category: Hydrolase]]
		+	[[Category: Rossmann fold]]

OCA at 09:54, 4 September 2013

OCA — Wed, 04 Sep 2013 09:54:29 GMT

←Older revision		Revision as of 09:54, 4 September 2013
Line 3:		Line 3:
	The entry 4lxh is ON HOLD		The entry 4lxh is ON HOLD

-	Authors: Bhowmik, S, Bolin, J.T.	+	Authors: Bhowmik, S., Bolin, J.T.

	Description: Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from Sphingomonas wittichii RW1, in complex with 3-Cl HOPDA		Description: Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from Sphingomonas wittichii RW1, in complex with 3-Cl HOPDA

OCA: Protected "4lxh" [edit=sysop:move=sysop]

OCA — Wed, 07 Aug 2013 20:19:53 GMT

Protected "4lxh" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:19, 7 August 2013

OCA: New page: '''Unreleased structure''' The entry 4lxh is ON HOLD Authors: Bhowmik, S, Bolin, J.T. Description: Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from S...

OCA — Wed, 07 Aug 2013 20:19:52 GMT

New page: '''Unreleased structure''' The entry 4lxh is ON HOLD Authors: Bhowmik, S, Bolin, J.T. Description: Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from S...

New page

'''Unreleased structure'''

The entry 4lxh is ON HOLD

Authors: Bhowmik, S, Bolin, J.T.

Description: Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from Sphingomonas wittichii RW1, in complex with 3-Cl HOPDA