By the same authors

From the same journal

The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase

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Author(s)

  • H L Schubert
  • K S Wilson
  • E Raux
  • S C Woodcock
  • M J Warren

Department/unit(s)

Publication details

JournalNature Structural Biology
DatePublished - Jul 1998
Issue number7
Volume5
Number of pages8
Pages (from-to)585-592
Original languageEnglish

Abstract

Biosynthesis of the corrin ring of vitamin B-12 requires the action of six S-adenosyl-L-methionine (AdoMet) dependent transmethylases, closely related in sequence. The first X-ray structure of one of these, cobalt-precorrin-4 transmethylase, CbiF, from Bacillus megaterium has been determined to a resolution of 2.4 Angstrom. CbiF contains two alpha/beta domains forming a trough in which S-adenosyl-L-homocysteine (AdoHcy) binds. The location of AdoHcy and a number of conserved residues, helps define the precorrin binding site. A second crystal form determined at 3.1 Angstrom resolution highlights the flexibility of two loops around this site. CbiF employs a unique mode of AdoHcy binding and represents a new class of transmethylase.

    Research areas

  • SALMONELLA-TYPHIMURIUM, PSEUDOMONAS-DENITRIFICANS, METHIONINE SYNTHASE, PROTEIN, VITAMIN-B-12, INTERMEDIATE, EXPRESSION, DOMAIN, GENES, B-12

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