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

Abstract:

Uridine at position 34 of bacterial transfer RNAs is commonly modified to uridine-5-oxyacetic acid (cmo(5)U) to increase the decoding capacity. The protein CmoA is involved in the formation of cmo(5)U 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 Å resolution and mass spectrometry demonstrate that it contains ...

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Publication status:
Published

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Publisher copy:
10.1107/s0907444913004939

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Journal:
Acta crystallographica. Section D, Biological crystallography
Volume:
69
Issue:
Pt 6
Pages:
1090-1098
Publication date:
2013-06-05
DOI:
EISSN:
1399-0047
ISSN:
0907-4449
URN:
uuid:70c270e2-dab3-4ebe-a953-113f770457c0
Source identifiers:
401242
Local pid:
pubs:401242

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