2uyq: Difference between revisions
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Revision as of 15:35, 30 October 2007
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CRYSTAL STRUCTURE OF ML2640C FROM MYCOBACTERIUM LEPRAE IN COMPLEX WITH S-ADENOSYLMETHIONINE
Overview
Mycobacterium leprae protein ML2640c belongs to a large family of, conserved hypothetical proteins predominantly found in mycobacteria, some, of them predicted as putative S-adenosylmethionine (AdoMet)-dependent, methyltransferases (MTase). As part of a Structural Genomics initiative on, conserved hypothetical proteins in pathogenic mycobacteria, we have, determined the structure of ML2640c in two distinct crystal forms. As, expected, ML2640c has a typical MTase core domain and binds the methyl, donor substrate AdoMet in a manner consistent with other known members of, this structural family. The putative acceptor substrate-binding site of, ML2640c is a large internal cavity, mostly lined by aromatic and aliphatic, side-chain residues, suggesting that a lipid-like molecule might be, ... [(full description)]
About this Structure
2UYQ is a [Single protein] structure of sequence from [Mycobacterium leprae] with SAM as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The crystal structure of M. leprae ML2640c defines a large family of putative S-adenosylmethionine-dependent methyltransferases in mycobacteria., Grana M, Haouz A, Buschiazzo A, Miras I, Wehenkel A, Bondet V, Shepard W, Schaeffer F, Cole ST, Alzari PM, Protein Sci. 2007 Sep;16(9):1896-904. Epub 2007 Jul 27. PMID:17660248
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