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1mo9

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[[Image:1mo9.gif|left|200px]]
 
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{{Structure
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==NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE COMPLEXED WITH 2-KETOPROPYL COENZYME M==
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|PDB= 1mo9 |SIZE=350|CAPTION= <scene name='initialview01'>1mo9</scene>, resolution 1.65&Aring;
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<StructureSection load='1mo9' size='340' side='right'caption='[[1mo9]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=KPC:(2-[2-KETOPROPYLTHIO]ETHANESULFONATE'>KPC</scene>
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<table><tr><td colspan='2'>[[1mo9]] 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=1MO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MO9 FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.65&#8491;</td></tr>
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|GENE=
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<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>, <scene name='pdbligand=KPC:(2-[2-KETOPROPYLTHIO]ETHANESULFONATE'>KPC</scene></td></tr>
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}}
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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=1mo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mo9 OCA], [https://pdbe.org/1mo9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mo9 RCSB], [https://www.ebi.ac.uk/pdbsum/1mo9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mo9 ProSAT]</span></td></tr>
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</table>
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'''NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE COMPLEXED WITH 2-KETOPROPYL COENZYME M'''
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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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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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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).
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1mo9_consurf.spt"</scriptWhenChecked>
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1MO9 is a [[Single protein]] structure of sequence 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=1MO9 OCA].
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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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==Reference==
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</jmolCheckbox>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12390015 12390015]
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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=1mo9 ConSurf].
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[[Category: Single protein]]
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<div style="clear:both"></div>
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[[Category: Xanthobacter sp.]]
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__TOC__
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[[Category: Clark, D D.]]
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</StructureSection>
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[[Category: Ensign, S A.]]
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[[Category: Large Structures]]
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[[Category: Jang, S B.]]
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[[Category: Xanthobacter autotrophicus Py2]]
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[[Category: Jeong, M S.]]
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[[Category: Clark DD]]
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[[Category: Nocek, B.]]
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[[Category: Ensign SA]]
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[[Category: Peters, J W.]]
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[[Category: Jang SB]]
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[[Category: FAD]]
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[[Category: Jeong MS]]
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[[Category: KPC]]
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[[Category: Nocek B]]
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[[Category: disulphide bond]]
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[[Category: Peters JW]]
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[[Category: nucleotide binding domain]]
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[[Category: nucleotide binding motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:46:00 2008''
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Current revision

NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE COMPLEXED WITH 2-KETOPROPYL COENZYME M

PDB ID 1mo9

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