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1req

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(New page: 200px<br /><applet load="1req" size="450" color="white" frame="true" align="right" spinBox="true" caption="1req, resolution 2.0&Aring;" /> '''METHYLMALONYL-COA MUT...)
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[[Image:1req.gif|left|200px]]<br /><applet load="1req" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1req, resolution 2.0&Aring;" />
 
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'''METHYLMALONYL-COA MUTASE'''<br />
 
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==Overview==
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==METHYLMALONYL-COA MUTASE==
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BACKGROUND. The enzyme methylmalonyl-coenzyme A (CoA) mutase, an alphabeta, heterodimer of 150 kDa, is a member of a class of enzymes that uses, coenzyme B12 (adenosylcobalamin) as a cofactor. The enzyme induces the, formation of an adenosyl radical from the cofactor. This radical then, initiates a free-radical rearrangement of its substrate, succinyl-CoA, to, methylmalonyl-CoA. RESULTS. Reported here is the crystal structure at 2 A, resolution of methylmalonyl-CoA mutase from Propionibacterium shermanii in, complex with coenzyme B12 and with the partial substrate desulpho-CoA, (lacking the succinyl group and the sulphur atom of the substrate). The, coenzyme is bound by a domain which shares a similar fold to those of, flavodoxin and the B12-binding domain of methylcobalamin-dependent, methionine synthase. The cobalt atom is coordinated, via a long bond, to a, histidine from the protein. The partial substrate is bound along the axis, of a (beta/alpha)8 TIM barrel domain. CONCLUSIONS. The histidine-cobalt, distance is very long (2.5 A compared with 1.95-2.2 A in free cobalamins), suggesting that the enzyme positions the histidine in order to weaken the, metal-carbon bond of the cofactor and favour the formation of the initial, radical species. The active site is deeply buried, and the only access to, it is through a narrow tunnel along the axis of the TIM barrel domain.
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<StructureSection load='1req' size='340' side='right'caption='[[1req]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1req]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1REQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1REQ FirstGlance]. <br>
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1REQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii] with B12, DCA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1REQ OCA].
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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&#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=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=DCA:DESULFO-COENZYME+A'>DCA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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==Reference==
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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=1req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1req OCA], [https://pdbe.org/1req PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1req RCSB], [https://www.ebi.ac.uk/pdbsum/1req PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1req ProSAT]</span></td></tr>
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How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution., Mancia F, Keep NH, Nakagawa A, Leadlay PF, McSweeney S, Rasmussen B, Bosecke P, Diat O, Evans PR, Structure. 1996 Mar 15;4(3):339-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8805541 8805541]
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</table>
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[[Category: Methylmalonyl-CoA mutase]]
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== Function ==
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[https://www.uniprot.org/uniprot/MUTB_PROFR MUTB_PROFR] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
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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/re/1req_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=1req ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Propionibacterium freudenreichii subsp. shermanii]]
[[Category: Propionibacterium freudenreichii subsp. shermanii]]
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[[Category: Protein complex]]
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[[Category: Evans PR]]
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[[Category: Evans, P.R.]]
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[[Category: Mancia F]]
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[[Category: Mancia, F.]]
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[[Category: B12]]
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[[Category: DCA]]
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[[Category: GOL]]
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[[Category: intramolecular transferase]]
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[[Category: isomerase]]
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[[Category: mutase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:31:58 2007''
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Current revision

METHYLMALONYL-COA MUTASE

PDB ID 1req

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