Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase
2010 (English)In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 277, no 19, 3947-3962 p.Article in journal (Refereed) Published
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 Å and at 2.8 Å, 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° 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.
Place, publisher, year, edition, pages
2010. Vol. 277, no 19, 3947-3962 p.
Mycobacterium smegmatis, methinoly-tRNA synthetase, methionine, adenosine
Biochemistry and Molecular Biology
Research subject Biology with specialization in Structural Biology
IdentifiersURN: urn:nbn:se:uu:diva-121752DOI: 10.1111/j.1742-4658.2010.07784.xISI: 000281850200008OAI: oai:DiVA.org:uu-121752DiVA: diva2:306462