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

Byrne, R.T.; Whelan, F.; Aller, P.; Bird, L.E.; Dowle, A.; Lobley, C.M.C.; Reddivari, Y.; Nettleship, J.E.; Owens, R.J.; Antson, A.A.; Waterman, D.G.

doi:10.1107/S0907444913004939

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 2
The overall structure of the CmoA dimer. (a) Two orthogonal views of the two monomers forming the dimer (green and blue ribbons). The S-adenosyl-S-carboxymethyl-L-homocysteine (SCM-SAH) cofactor is shown with O atoms in red, N atoms in blue and C atoms in green. (b) The SEC-SLS chromatogram that confirms that CmoA is a dimer in solution. The refractive index (RI; red line) and right-angle light scattering (RALS; green line) traces are displayed. The molecular weight calculated by the OmniSEC software (MW; black line) is shown above the elution peak. The dispersity, Mw/Mn, defined as the ratio of the weight average to number average molecular weights was reported to be 1.001, indicating a highly uniform sample.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 69| Part 6| June 2013| Pages 1090-1098

https://doi.org/10.1107/S0907444913004939

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