2X1M

Flexibility and Communication within the Structure of the Mycobacterium Smegmatis Methionyl-tRNA Synthetase.

(2010) FEBS J 277: 3947

• PubMed: 20796028 Search on PubMed
• DOI: https://doi.org/10.1111/j.1742-4658.2010.07784.x
• Primary Citation of Related Structures:  
  2X1L, 2X1M


• PubMed Abstract: 
  

  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 ? and at 2.8 ?, 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.

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Organizational Affiliation: 

Department of Cell and Molecular Biology, Uppsala Biomedical Center, Uppsala University, Uppsala, Sweden.