1i1h
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CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE COMPLEX WITH HYDROGENOBYRINIC ACID
OverviewOverview
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.
About this StructureAbout this Structure
1I1H is a Single protein structure of sequence from Pseudomonas denitrificans with COJ as ligand. Active as Precorrin-8X methylmutase, with EC number 5.4.1.2 Full crystallographic information is available from OCA.
ReferenceReference
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
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