3q6j

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{{STRUCTURE_3q6j| PDB=3q6j | SCENE= }}
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==Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M Oxidoreductase/Carboxylase==
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===Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M Oxidoreductase/Carboxylase===
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<StructureSection load='3q6j' size='340' side='right' caption='[[3q6j]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
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{{ABSTRACT_PUBMED_21192936}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3q6j]] is a 2 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=3Q6J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q6J FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=KPC:(2-[2-KETOPROPYLTHIO]ETHANESULFONATE'>KPC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c3d|2c3d]], [[1mo9|1mo9]], [[1mok|1mok]]</td></tr>
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<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>
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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=3q6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q6j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q6j RCSB], [http://www.ebi.ac.uk/pdbsum/3q6j PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) has been determined in a state in which CO(2) is observed providing insights into the mechanism of carboxylation. In the substrate encapsulated state of the enzyme, CO(2) is bound at the base of a narrow hydrophobic substrate access channel. The base of the channel is demarcated by a transition from a hydrophobic to hydrophilic environment where CO(2) is located in position for attack on the carbanion of the ketopropyl group of the substrate to ultimately produce acetoacetate. This binding mode effectively discriminates against H(2)O and prevents protonation of the ketopropyl leaving group. STRUCTURED SUMMARY: 2-KPCCbinds to 2-KPCC by x-ray crystallography (View interaction).
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==Function==
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Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase.,Pandey AS, Mulder DW, Ensign SA, Peters JW FEBS Lett. 2011 Feb 4;585(3):459-64. Epub 2010 Dec 27. PMID:21192936<ref>PMID:21192936</ref>
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[[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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[3q6j]] is a 2 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=3Q6J OCA].
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</div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:021192936</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Xanthobacter autotrophicus]]
[[Category: Xanthobacter autotrophicus]]
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[[Category: Ensign, S A.]]
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[[Category: Ensign, S A]]
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[[Category: Mulder, D W.]]
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[[Category: Mulder, D W]]
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[[Category: Pandey, A S.]]
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[[Category: Pandey, A S]]
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[[Category: Peters, J W.]]
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[[Category: Peters, J W]]
[[Category: Carbon dioxide]]
[[Category: Carbon dioxide]]
[[Category: Carboxylase]]
[[Category: Carboxylase]]

Revision as of 10:22, 19 December 2014

Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M Oxidoreductase/Carboxylase

3q6j, resolution 1.92Å

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