TAILIEUCHUNG - Báo cáo khoa học: Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase Henrik Ingvarsson and Torsten Unge

Two structures of monomeric methionyl-tRNA synthetase, fromMycobac-terium smegmatis, in complex with the ligands methionine⁄adenosine and methionine, were analyzed by X-ray crystallography at A˚ and at 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. | ỊFEBS Journal Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase Henrik Ingvarsson and Torsten Unge Department of Celland Molecular Biology Uppsala BiomedicalCenter Uppsala University Sweden Keywords adenosine methionine methionyl-tRNA synthetase MetRS Mycobacterium smegmatis Correspondence T. Unge Department of Celland Molecular Biology Uppsala BiomedicalCenter Uppsala University Box 596 SE-751 24 Uppsala Sweden Fax 46 18 53 69 71 Tel 46 18 471 50 62 E-mail torsten@ Database Structural data are available in the Protein Data Bank BioMagResBank databases under the accession numbers 2X1L for M. smegmatis MetRS M A and 2X1M for M. smegmatis MetRS M Received 17 May 2010 revised 15 July 2010 accepted 20 July 2010 doi 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 A and at 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 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. Introduction With the aim of developing a new anti-tuberculosis drug we selected methionyl-tRNA synthetase MetRS as a potential target. The aminoacyl-tRNA synthetases aaRSs have been .

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