2br4
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(New page: 200px<br /> <applet load="2br4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2br4, resolution 2.59Å" /> '''CMCI-D160 MG-SAM'''...)
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Revision as of 19:55, 29 October 2007
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CMCI-D160 MG-SAM
Overview
Cephamycin C-producing microorganisms use two enzymes to convert, cephalosporins to their 7alpha-methoxy derivatives. Here we report the, X-ray structure of one of these enzymes, CmcI, from Streptomyces, clavuligerus. The polypeptide chain of the enzyme folds into a C-terminal, Rossmann domain and a smaller N-terminal domain, and the molecule packs as, a hexamer in the crystal. The Rossmann domain binds, S-adenosyl-L-methionine (SAM) and the demethylated product, S-adenosyl-L-homocysteine, in a fashion similar to the common binding mode, of this cofactor in SAM-dependent methyltransferases. There is a, magnesium-binding site in the vicinity of the SAM site with a bound, magnesium ion ligated by residues Asp160, Glu186 and Asp187. The expected, cephalosporin binding site near the magnesium ... [(full description)]
About this Structure
2BR4 is a [Single protein] structure of sequence from [Streptomyces clavuligerus] with MG, SAM, P4C and PEG as [ligands]. Full crystallographic information is available from [OCA].
Reference
Insights into cephamycin biosynthesis: the crystal structure of CmcI from Streptomyces clavuligerus., Oster LM, Lester DR, Terwisscha van Scheltinga A, Svenda M, van Lun M, Genereux C, Andersson I, J Mol Biol. 2006 Apr 28;358(2):546-58. Epub 2006 Feb 21. PMID:16527306
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