2c3c

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[[Image:2c3c.png|left|200px]]
 
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==2.01 Angstrom X-ray crystal structure of a mixed disulfide between coenzyme M and NADPH-dependent oxidoreductase 2-ketopropyl coenzyme M carboxylase==
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The line below this paragraph, containing "STRUCTURE_2c3c", creates the "Structure Box" on the page.
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<StructureSection load='2c3c' size='340' side='right'caption='[[2c3c]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2c3c]] is a 2 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=2C3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C3C FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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{{STRUCTURE_2c3c| PDB=2c3c | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c3c OCA], [https://pdbe.org/2c3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c3c RCSB], [https://www.ebi.ac.uk/pdbsum/2c3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c3c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c3/2c3c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2c3c ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of the mixed, enzyme-cofactor disulfide intermediate of ketopropyl-coenzyme M oxidoreductase/carboxylase has been determined by X-ray diffraction methods. Ketopropyl-coenzyme M oxidoreductase/carboxylase belongs to a family of pyridine nucleotide-containing flavin-dependent disulfide oxidoreductases, which couple the transfer of hydride derived from the NADPH to the reduction of protein cysteine disulfide. Ketopropyl-coenzyme M oxidoreductase/carboxylase, a unique member of this enzyme class, catalyzes thioether bond cleavage of the substrate, 2-ketopropyl-coenzyme M, and carboxylation of what is thought to be an enzyme-stabilized enolacetone intermediate. The mixed disulfide of 2-ketopropyl-coenzyme M oxidoreductase/carboxylase was captured through crystallization of the enzyme with the physiological products of the reaction, acetoacetate, coenzyme M, and NADP, and reduction of the crystals with dithiothreitol just prior to data collection. Density in the active-site environment consistent with acetone, the product of reductive decarboxylation of acetoacetate, was revealed in this structure in addition to a well-defined hydrophobic pocket or channel that could be involved in the access for carbon dioxide. The analysis of this structure and that of a coenzyme-M-bound form provides insights into the stabilization of intermediates, substrate carboxylation, and product release.
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===2.01 ANGSTROM X-RAY CRYSTAL STRUCTURE OF A MIXED DISULFIDE BETWEEN COENZYME M AND NADPH-DEPENDENT OXIDOREDUCTASE 2-KETOPROPYL COENZYME M CARBOXYLASE===
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Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.,Pandey AS, Nocek B, Clark DD, Ensign SA, Peters JW Biochemistry. 2006 Jan 10;45(1):113-20. PMID:16388586<ref>PMID:16388586</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16388586}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2c3c" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16388586 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16388586}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2C3C is a [[Single protein]] structure of 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=2C3C OCA].
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[[Category: Xanthobacter autotrophicus Py2]]
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[[Category: Clark DD]]
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==Reference==
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[[Category: Ensign SA]]
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Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase., Pandey AS, Nocek B, Clark DD, Ensign SA, Peters JW, Biochemistry. 2006 Jan 10;45(1):113-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16388586 16388586]
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[[Category: Nocek B]]
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[[Category: Single protein]]
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[[Category: Pandey AS]]
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[[Category: Xanthobacter autotrophicus]]
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[[Category: Peters JW]]
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[[Category: Clark, D D.]]
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[[Category: Ensign, S A.]]
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[[Category: Nocek, B.]]
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[[Category: Pandey, A S.]]
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[[Category: Peters, J W.]]
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[[Category: Coenzyme m]]
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[[Category: Fad]]
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[[Category: Mixed disulfide]]
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[[Category: Oxidoreductase]]
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[[Category: Redox-active center]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:53:35 2008''
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Current revision

2.01 Angstrom X-ray crystal structure of a mixed disulfide between coenzyme M and NADPH-dependent oxidoreductase 2-ketopropyl coenzyme M carboxylase

PDB ID 2c3c

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