1i1h

<StructureSection load='1i1h' size='340' side='right' caption='[[1i1h]], [[Resolution|resolution]] 2.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[1i1h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_denitrificans"_(christensen_1903)_bergey_et_al._1923,_nom._rejic. "pseudomonas denitrificans" (christensen 1903) bergey et al. 1923, nom. rejic.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I1H FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COJ:HYDROGENOBYRINIC+ACID'>COJ</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f2v|1f2v]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COBH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43306 "Pseudomonas denitrificans" (Christensen 1903) Bergey et al. 1923, nom. rejic.])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Precorrin-8X_methylmutase Precorrin-8X methylmutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.61 5.4.99.61] </span></td></tr>

<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=1i1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1h OCA], [http://pdbe.org/1i1h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i1h RCSB], [http://www.ebi.ac.uk/pdbsum/1i1h PDBsum]</span></td></tr>

[[http://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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i1/1i1h_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1i1h" style="background-color:#fffaf0;"></div>

[[Category: Precorrin-8X methylmutase]]

[[Category: Li, D]]

[[Category: Roessner, C A]]

[[Category: Sacchettini, J C]]

[[Category: Scott, A I]]

[[Category: Shipman, L W]]

[[Category: Vitamin b12]]