2x1m

Publication Abstract from PubMed

Two structures of monomeric methionyl-tRNA synthetase, from Mycobacterium smegmatis, in complex with the ligands methionine/adenosine and methionine, were analyzed by X-ray crystallography at 2.3 A and at 2.8 A, respectively. The structures demonstrated the flexibility of the multidomain enzyme. A new conformation of the structure was identified in which the connective peptide domain bound more closely to the catalytic domain than described previously. The KMSKS(301-305) loop in our structures was in an open and inactive conformation that differed from previous structures by a rotation of the loop of about 90 degrees around hinges located at Asn297 and Val310. The binding of adenosine to the methionyl-tRNA synthetase methionine complex caused a shift in the KMSKS domain that brought it closer to the catalytic domain. The potential use of the adenosine-binding site for inhibitor binding was evaluated and a potential binding site for a specific allosteric inhibitor was identified.

Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase.,Ingvarsson H, Unge T FEBS J. 2010 Aug 26. PMID:20796028^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.