Cloning, purification and preliminary crystallographic analysis of cobalamin methyltransferases from Rhodobacter capsulatus

Arefeh Seyedarabi, Thomas Hutchison, Teng Teng To, Evelyne Deery, Amanda Brindley, Martin J. Warren, Richard W. Pickersgill

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


Of the 30 biosynthetic steps necessary for the production of cobalamin (vitamin B12), eight involve the addition of S-adenosylmethionine-derived methyl groups to the tetrapyrrole framework. These eight methyl additions are catalysed by six canonical methyltransferase domains and one noncanonical methyltransferase domain. Recombinant forms of four methyltransferases from Rhodobacter capsulatus, CobJ, CobM, CobF and CobL, and of the C-terminal noncanonical domain of CobL (CobL-C) have been crystallized, some in more than one crystal form. Most of the crystals diffracted to beyond 2.5 Å resolution and all are suitable for structure determination. Crystals of CobM and CobJ, which are involved in ring contraction, and of CobL, which is involved in two methylations and decarboxylation, are reported for the first time.

Original languageEnglish
Pages (from-to)1652-1656
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number12
Publication statusPublished - Dec 2010


  • cobalamin methyltransferases
  • CobF
  • CobJ
  • CobL
  • CobM
  • Rhodobacter capsulatus

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