1mok - Revision history

OCA at 08:38, 10 April 2024

2024-04-10T08:38:51Z

←Older revision		Revision as of 08:38, 10 April 2024
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	<StructureSection load='1mok' size='340' side='right'caption='[[1mok]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1mok' size='340' side='right'caption='[[1mok]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1mok]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Xanp2 Xanp2~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MOK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1mok]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthobacter_autotrophicus_Py2 Xanthobacter autotrophicus Py2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MOK FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FAD:FLAVIN~~-~~ADENINE+DINUCLEOTIDE'>FAD</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]] 2.8Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1mo9\|1mo9]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>[https://en.wikipedia.org/wiki/2-oxopropyl-CoM_reductase_(carboxylating) 2-oxopropyl-CoM reductase (carboxylating)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.5 1.8.1.5] </~~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=1mok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mok OCA], [https://pdbe.org/1mok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mok RCSB], [https://www.ebi.ac.uk/pdbsum/1mok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mok 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=1mok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mok OCA], [https://pdbe.org/1mok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mok RCSB], [https://www.ebi.ac.uk/pdbsum/1mok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mok ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/XECC_XANP2 XECC_XANP2]] Catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M.	+	[https://www.uniprot.org/uniprot/XECC_XANP2 XECC_XANP2] Catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mok 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=1mok ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC) is the terminal enzyme in a metabolic pathway that results in the conversion of propylene to the central metabolite acetoacetate in Xanthobacter autotrophicus Py2. This enzyme is an FAD-containing enzyme that is a member of the NADPH:disulfide oxidoreductase (DSOR) family of enzymes that include glutathione reductase, dihydrolipoamide dehydrogenase, trypanothione reductase, thioredoxin reductase, and mercuric reductase. In contrast to the prototypical reactions catalyzed by members of the DSOR family, the NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M. The structure of 2-KPCC reveals a unique active site in comparison to those of other members of the DSOR family of enzymes and demonstrates how the enzyme architecture has been adapted for the more sophisticated biochemical reaction. In addition, comparison of the structures in the native state and in the presence of bound substrate indicates the binding of the substrate 2-ketopropyl-coenzyme M induces a conformational change resulting in the collapse of the substrate access channel. The encapsulation of the substrate in this manner is reminiscent of the conformational changes observed in the well-characterized CO2-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxidase (Rubisco).
-
-	Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.,Nocek B, Jang SB, Jeong MS, Clark DD, Ensign SA, Peters JW Biochemistry. 2002 Oct 29;41(43):12907-13. PMID:12390015<ref>PMID:12390015</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1mok" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Xanp2~~]]	+	[[Category: Xanthobacter autotrophicus Py2]]
-	[[Category: Clark~~, D D~~]]	+	[[Category: Clark DD]]
-	[[Category: Ensign~~, S A~~]]	+	[[Category: Ensign SA]]
-	[[Category: Jang~~, S B~~]]	+	[[Category: Jang SB]]
-	[[Category: Jeong~~, M S~~]]	+	[[Category: Jeong MS]]
-	[[Category: Nocek, B]]	+	[[Category: Nocek B]]
-	[[Category: Peters~~, J W]]~~	+	[[Category: Peters JW]]
-	~~[[Category: Nucleotide binding domain]]~~	+
-	~~[[Category: Nucleotide binding motif]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 08:54, 21 April 2021

2021-04-21T08:54:40Z

←Older revision		Revision as of 08:54, 21 April 2021
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	<StructureSection load='1mok' size='340' side='right'caption='[[1mok]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1mok' size='340' side='right'caption='[[1mok]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1mok]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Xanp2 Xanp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1MOK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1mok]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanp2 Xanp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MOK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mo9\|1mo9]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mo9\|1mo9]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/2-oxopropyl-CoM_reductase_(carboxylating) 2-oxopropyl-CoM reductase (carboxylating)], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.5 1.8.1.5] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/2-oxopropyl-CoM_reductase_(carboxylating) 2-oxopropyl-CoM reductase (carboxylating)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.5 1.8.1.5] </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=1mok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mok OCA], [~~http~~://pdbe.org/1mok PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1mok RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1mok PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1mok 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=1mok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mok OCA], [https://pdbe.org/1mok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mok RCSB], [https://www.ebi.ac.uk/pdbsum/1mok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mok ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/XECC_XANP2 XECC_XANP2]] Catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M.	+	[[https://www.uniprot.org/uniprot/XECC_XANP2 XECC_XANP2]] Catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 12:55, 17 July 2019

2019-07-17T12:55:56Z

←Older revision		Revision as of 12:55, 17 July 2019
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	==NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE==		==NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE==
-	<StructureSection load='1mok' size='340' side='right' caption='[[1mok]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='1mok' size='340' side='right'caption='[[1mok]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1mok]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanp2 Xanp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOK FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mok]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanp2 Xanp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOK FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1mok_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1mok_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 34:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Xanp2]]		[[Category: Xanp2]]
	[[Category: Clark, D D]]		[[Category: Clark, D D]]

OCA at 14:50, 12 October 2017

2017-10-12T14:50:33Z

←Older revision		Revision as of 14:50, 12 October 2017
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		+
	==NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE==		==NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE==
	<StructureSection load='1mok' size='340' side='right' caption='[[1mok]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1mok' size='340' side='right' caption='[[1mok]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1mok]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Xanthobacter_autotrophicus Xanthobacter autotrophicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1mok]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanp2 Xanp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOK FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mo9\|1mo9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mo9\|1mo9]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-oxopropyl-CoM_reductase_(carboxylating) 2-oxopropyl-CoM reductase (carboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.5 1.8.1.5] </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-oxopropyl-CoM_reductase_(carboxylating) 2-oxopropyl-CoM reductase (carboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.5 1.8.1.5] </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=1mok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mok OCA], [http://pdbe.org/1mok PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mok RCSB], [http://www.ebi.ac.uk/pdbsum/1mok 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=1mok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mok OCA], [http://pdbe.org/1mok PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mok RCSB], [http://www.ebi.ac.uk/pdbsum/1mok PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mok ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	<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=1mok ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Xanthobacter autotrophicus~~]]	+	[[Category: Xanp2]]
	[[Category: Clark, D D]]		[[Category: Clark, D D]]
	[[Category: Ensign, S A]]		[[Category: Ensign, S A]]

OCA at 01:59, 12 September 2015

2015-09-12T01:59:44Z

←Older revision		Revision as of 01:59, 12 September 2015
Line 6:		Line 6:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mo9\|1mo9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mo9\|1mo9]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-oxopropyl-CoM_reductase_(carboxylating) 2-oxopropyl-CoM reductase (carboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.5 1.8.1.5] </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-oxopropyl-CoM_reductase_(carboxylating) 2-oxopropyl-CoM reductase (carboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.5 1.8.1.5] </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=1mok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mok OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mok RCSB], [http://www.ebi.ac.uk/pdbsum/1mok 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=1mok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mok OCA], [http://pdbe.org/1mok PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mok RCSB], [http://www.ebi.ac.uk/pdbsum/1mok PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 1mok" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 22:22, 25 December 2014

2014-12-25T22:22:41Z

←Older revision		Revision as of 22:22, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1mok]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOK FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mok]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOK FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mo9\|1mo9]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mo9\|1mo9]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-oxopropyl-CoM_reductase_(carboxylating) 2-oxopropyl-CoM reductase (carboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.5 1.8.1.5] </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-oxopropyl-CoM_reductase_(carboxylating) 2-oxopropyl-CoM reductase (carboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.5 1.8.1.5] </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=1mok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mok OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mok RCSB], [http://www.ebi.ac.uk/pdbsum/1mok 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=1mok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mok OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mok RCSB], [http://www.ebi.ac.uk/pdbsum/1mok PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/XECC_XANP2 XECC_XANP2]] Catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Xanthobacter autotrophicus]]		[[Category: Xanthobacter autotrophicus]]
-	[[Category: Clark, D D.]]	+	[[Category: Clark, D D]]
-	[[Category: Ensign, S A.]]	+	[[Category: Ensign, S A]]
-	[[Category: Jang, S B.]]	+	[[Category: Jang, S B]]
-	[[Category: Jeong, M S.]]	+	[[Category: Jeong, M S]]
-	[[Category: Nocek, B.]]	+	[[Category: Nocek, B]]
-	[[Category: Peters, J W.]]	+	[[Category: Peters, J W]]
	[[Category: Nucleotide binding domain]]		[[Category: Nucleotide binding domain]]
	[[Category: Nucleotide binding motif]]		[[Category: Nucleotide binding motif]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 11:29, 3 October 2014

2014-10-03T11:29:07Z

←Older revision		Revision as of 11:29, 3 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1mok\| PDB=1mok \| SCENE= }}~~	+	==NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE==
-	===NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE===	+	<StructureSection load='1mok' size='340' side='right' caption='[[1mok]], [[Resolution\|resolution]] 2.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_12390015}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1mok]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOK FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mo9\|1mo9]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-oxopropyl-CoM_reductase_(carboxylating) 2-oxopropyl-CoM reductase (carboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.5 1.8.1.5] </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=1mok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mok OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mok RCSB], [http://www.ebi.ac.uk/pdbsum/1mok 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/mo/1mok_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 ==
		+	The NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC) is the terminal enzyme in a metabolic pathway that results in the conversion of propylene to the central metabolite acetoacetate in Xanthobacter autotrophicus Py2. This enzyme is an FAD-containing enzyme that is a member of the NADPH:disulfide oxidoreductase (DSOR) family of enzymes that include glutathione reductase, dihydrolipoamide dehydrogenase, trypanothione reductase, thioredoxin reductase, and mercuric reductase. In contrast to the prototypical reactions catalyzed by members of the DSOR family, the NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M. The structure of 2-KPCC reveals a unique active site in comparison to those of other members of the DSOR family of enzymes and demonstrates how the enzyme architecture has been adapted for the more sophisticated biochemical reaction. In addition, comparison of the structures in the native state and in the presence of bound substrate indicates the binding of the substrate 2-ketopropyl-coenzyme M induces a conformational change resulting in the collapse of the substrate access channel. The encapsulation of the substrate in this manner is reminiscent of the conformational changes observed in the well-characterized CO2-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxidase (Rubisco).

-	~~==Function==~~	+	Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.,Nocek B, Jang SB, Jeong MS, Clark DD, Ensign SA, Peters JW Biochemistry. 2002 Oct 29;41(43):12907-13. PMID:12390015<ref>PMID:12390015</ref>
-	~~[[http://www.uniprot.org/uniprot/XECC_XANP2 XECC_XANP2]] Catalyzes the reductive cleavage~~ of the ~~thioether linkage~~ of 2-ketopropyl-coenzyme M, ~~and the subsequent carboxylation of the ketopropyl cleavage product~~, ~~yielding the products acetoacetate and free coenzyme M~~.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[1mok]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:012390015</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Xanthobacter autotrophicus]]		[[Category: Xanthobacter autotrophicus]]
	[[Category: Clark, D D.]]		[[Category: Clark, D D.]]

OCA at 10:29, 16 April 2014

2014-04-16T10:29:19Z

←Older revision		Revision as of 10:29, 16 April 2014
Line 1:		Line 1:
-	[[Image:1mok.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_1mok", 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_1mok\| PDB=1mok \| SCENE= }}		{{STRUCTURE_1mok\| PDB=1mok \| SCENE= }}
-
	===NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE===		===NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE===
		+	{{ABSTRACT_PUBMED_12390015}}

-		+	==Function==
-	~~<!--~~	+	[[http://www.uniprot.org/uniprot/XECC_XANP2 XECC_XANP2]] Catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M.
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_12390015}}, adds the Publication Abstract to the page~~	+
-	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov)~~, ~~where 12390015 is~~ the ~~PubMed ID number~~.	+
-	~~-->~~	+
-	~~{{ABSTRACT_PUBMED_12390015}}~~	+

	==About this Structure==		==About this Structure==
Line 22:		Line 10:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:012390015</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012390015</ref><references group="xtra"/><references/>
	[[Category: Xanthobacter autotrophicus]]		[[Category: Xanthobacter autotrophicus]]
	[[Category: Clark, D D.]]		[[Category: Clark, D D.]]

OCA: Protected "1mok" [edit=sysop:move=sysop]

2012-05-09T08:10:08Z

Protected "1mok" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:10, 9 May 2012

OCA at 08:10, 9 May 2012

2012-05-09T08:10:07Z

←Older revision		Revision as of 08:10, 9 May 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1mok.png\|left\|200px]]		[[Image:1mok.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~1MOK~~ is a 4 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/~~Xanthobacter_sp.~~ Xanthobacter ~~sp.~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA].	+	[[1mok]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~12390015~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012390015</ref><references group="xtra"/>
-	[[Category: Xanthobacter ~~sp.~~]]	+	[[Category: Xanthobacter autotrophicus]]
	[[Category: Clark, D D.]]		[[Category: Clark, D D.]]
	[[Category: Ensign, S A.]]		[[Category: Ensign, S A.]]
Line 31:		Line 30:
	[[Category: Nocek, B.]]		[[Category: Nocek, B.]]
	[[Category: Peters, J W.]]		[[Category: Peters, J W.]]
-	[[Category: Disulphide bond]]
	[[Category: Nucleotide binding domain]]		[[Category: Nucleotide binding domain]]
	[[Category: Nucleotide binding motif]]		[[Category: Nucleotide binding motif]]
-		+	[[Category: Oxidoreductase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Wed Feb 18 09:38:43 2009''~~	+