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From the same journal

S-Adenosyl-S-carboxymethyl-l-homocysteine: a novel cofactor found in the putative tRNA-modifying enzyme CmoA

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Published copy (DOI)


  • Robert T. Byrne
  • Fiona Whelan
  • Pierre Aller
  • Louise E. Bird
  • Adam Dowle
  • Carina M C Lobley
  • Yamini Reddivari
  • Joanne E. Nettleship
  • Raymond J. Owens
  • Alfred A. Antson
  • David G. Waterman


Publication details

JournalActa Crystallographica Section D: Biological Crystallography
DateE-pub ahead of print - 15 May 2013
DatePublished (current) - 1 Jun 2013
Issue number6
Number of pages9
Pages (from-to)1090-1098
Early online date15/05/13
Original languageEnglish


Uridine at position 34 of bacterial transfer RNAs is commonly modified to uridine-5-oxyacetic acid (cmo5U) to increase the decoding capacity. The protein CmoA is involved in the formation of cmo5U and was annotated as an S-adenosyl-l-methionine-dependent (SAM-dependent) methyltransferase on the basis of its sequence homology to other SAM-containing enzymes. However, both the crystal structure of Escherichia coli CmoA at 1.73 14;Å resolution and mass spectrometry demonstrate that it contains a novel cofactor, S-adenosyl-S-carboxymethyl-l-homocysteine (SCM-SAH), in which the donor methyl group is substituted by a carboxymethyl group. The carboxyl moiety forms a salt-bridge interaction with Arg199 that is conserved in a large group of CmoA-related proteins but is not conserved in other SAM-containing enzymes. This raises the possibility that a number of enzymes that have previously been annotated as SAM-dependent are in fact SCM-SAH-dependent. Indeed, inspection of electron density for one such enzyme with known X-ray structure, PDB entry 1im8, suggests that the active site contains SCM-SAH and not SAM.

    Research areas

  • cmoU biosynthesis, Escherichia coli, putative tRNA-modification enzyme, SCM-SAH

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