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Related Experiment Videos

Crystal structure of precorrin-8x methyl mutase.

L W Shipman1, D Li, C A Roessner

  • 1Department of Chemistry, Texas A&M University, College Station, TX 77843, USA. sacchett@tamu.edu

Structure (London, England : 1993)
|July 27, 2001
PubMed
Summary

Precorrin-8x methyl mutase (CobH) crystal structure reveals a [1,5]-sigmatropic shift mechanism for vitamin B12 synthesis. This enzyme facilitates methyl group migration via a conserved histidine residue within its active site.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Investigates the aerobic pathway for vitamin B12 biosynthesis.
  • Focuses on the enzyme precorrin-8x methyl mutase (CobH).
  • Examines the mechanism of methyl migration in precorrin-8x.

Purpose of the Study:

  • To elucidate the structural basis of the [1,5]-sigmatropic methyl shift catalyzed by CobH.
  • To understand how CobH selects a specific tautomer of precorrin-8x for catalysis.
  • To identify key residues involved in the methyl migration process.

Main Methods:

  • X-ray crystallography of precorrin-8x methyl mutase (CobH).
  • Structural analysis of the enzyme-substrate/product complex.
  • Bioinformatic analysis to identify conserved residues.

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Main Results:

  • The dimeric structure of CobH forms shared active sites that discriminate tautomers.
  • A conserved histidine residue is located near the methyl migration site in ring C.
  • The crystal structure provides evidence for a [1,5]-sigmatropic shift of a methyl group.

Conclusions:

  • The [1,5]-sigmatropic shift mechanism is supported by the CobH crystal structure.
  • Protonation of the ring C nitrogen precedes methyl migration.
  • CobH facilitates the conversion of precorrin-8x to hydrogenobyrinic acid.