Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein
Article Abstract:
The structure of CspB, one of the major cold-shock proteins, obtained by a sudden drop in growth temperature in both Escherichia coli and Bacillus subtilis, is ascertained on the basis of two crystal forms. CspB exists in both the crystal forms as an antiparallel five stranded beta-barrel. In the three consecutive beta-strands, the central strand which contains the RNP1 motif produces a rich surface of aromatic and basic residues that may be participating in nucleic acid binding.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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BluB cannibalizes flavin to form the lower ligand of vitamin [B.sub.12]
Article Abstract:
A study was conducted to show that BluB gene found in Sinorhizobium meliloti triggers the unprecedented fragmentation and contraction of the bound flavin mononucleotide cofactor and cleavage of the ribityl tail to form 5,6-dimethylbenzimidazole (DMB) and D-erythrose 4-phosphate. The findings suggest that BluB is hybrid enzyme with structural similarity to the flavin oxidoreductases and functional relatedness to the mono-oxygenases.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
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Peptide cyclization catalysed by the thioesterase domain of tyrocidine synthetase
Article Abstract:
Research is presented concerning the efficient catalysis of a decapeptide-thioester by the action of the carboxy-terminal thioesterase domain to result in the formation of of the antibiotic tyrocidine A.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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