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2uyq

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[[Category: transferase]]
[[Category: transferase]]
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Revision as of 16:36, 5 November 2007

Image:2uyq.gif

2uyq, resolution 1.80Å

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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, targeted for catalysis. A flap segment (residues 222-256), which isolates, the binding site from the bulk solvent and is highly mobile in the crystal, structures, could serve as a gateway to allow substrate entry and product, release. The multiple sequence alignment of ML2640c-like proteins revealed, that the central alpha/beta core and the AdoMet-binding site are very well, conserved within the family. However, the amino acid positions defining, the binding site for the acceptor substrate display a higher variability, suggestive of distinct acceptor substrate specificities. The ML2640c, crystal structures offer the first structural glimpses at this important, family of mycobacterial proteins and lend strong support to their, functional assignment as AdoMet-dependent methyltransferases.

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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