1f2v

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Current revision (07:10, 7 February 2024) (edit) (undo)
 
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<StructureSection load='1f2v' size='340' side='right'caption='[[1f2v]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1f2v' size='340' side='right'caption='[[1f2v]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1f2v]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1f2v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_denitrificans_(nom._rej.) Pseudomonas denitrificans (nom. rej.)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2V FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Precorrin-8X_methylmutase Precorrin-8X methylmutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.61 5.4.99.61] </span></td></tr>
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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]] 2.1&#8491;</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=1f2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2v OCA], [https://pdbe.org/1f2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2v RCSB], [https://www.ebi.ac.uk/pdbsum/1f2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2v 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=1f2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2v OCA], [https://pdbe.org/1f2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2v RCSB], [https://www.ebi.ac.uk/pdbsum/1f2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/COBH_PSEDE COBH_PSEDE]] Catalyzes the conversion of precorrin-8X to hydrogenobyrinic acid; a methyl migration reaction during the transformation of precorrin-3 to form cobyrinic acid.
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[https://www.uniprot.org/uniprot/COBH_SINSX COBH_SINSX] Catalyzes the conversion of precorrin-8X to hydrogenobyrinate.<ref>PMID:1732194</ref>
== 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=1f2v 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=1f2v ConSurf].
<div style="clear:both"></div>
<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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BACKGROUND: The crystal structure of precorrin-8x methyl mutase (CobH), an enzyme of the aerobic pathway to vitamin B12, provides evidence that the mechanism for methyl migration can plausibly be regarded as an allowed [1,5]-sigmatropic shift of a methyl group from C-11 to C-12 at the C ring of precorrin-8x to afford hydrogenobyrinic acid. RESULTS: The dimeric structure of CobH creates a set of shared active sites that readily discriminate between different tautomers of precorrin-8x and select a discrete tautomer for sigmatropic rearrangement. The active site contains a strictly conserved histidine residue close to the site of methyl migration in ring C of the substrate. CONCLUSION: Analysis of the structure with bound product suggests that the [1,5]-sigmatropic shift proceeds by protonation of the ring C nitrogen, leading to subsequent methyl migration.
 
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Crystal structure of precorrin-8x methyl mutase.,Shipman LW, Li D, Roessner CA, Scott AI, Sacchettini JC Structure. 2001 Jul 3;9(7):587-96. PMID:11470433<ref>PMID:11470433</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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<div class="pdbe-citations 1f2v" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Precorrin-8X methylmutase]]
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[[Category: Li D]]
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[[Category: Li, D]]
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[[Category: Roessner CA]]
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[[Category: Roessner, C A]]
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[[Category: Sacchettini JC]]
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[[Category: Sacchettini, J C]]
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[[Category: Scott AI]]
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[[Category: Scott, A I]]
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[[Category: Shipman LW]]
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[[Category: Shipman, L W]]
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[[Category: Alpha-beta wind]]
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[[Category: Doubly wound sheet]]
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[[Category: Isomerase]]
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Current revision

CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE OF AEROBIC VITAMIN B12 SYNTHESIS

PDB ID 1f2v

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