2X1M

Crystal structure of Mycobacterium smegmatis methionyl-tRNA synthetase in complex with methionine

Summary for 2X1M

• Entry DOI: 10.2210/pdb2x1m/pdb
• Related: 2X1L
• Descriptor: METHIONYL-TRNA SYNTHETASE, METHIONINE, DIHYDROGENPHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: nucleotide-binding, protein biosynthesis, ligase, aminoacyl-trna synthetase
• Biological source: MYCOBACTERIUM SMEGMATIS
• Total number of polymer chains: 1
• Total formula weight: 59642.73

Authors

Ingvarsson, H.,Jones, T.A.,Unge, T. (deposition date: 2009-12-31, release date: 2010-07-28, Last modification date: 2023-12-20)

Primary citation

Ingvarsson, H.,Unge, T.
Flexibility and Communication within the Structure of the Mycobacterium Smegmatis Methionyl-tRNA Synthetase.
FEBS J., 277:3947-, 2010

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 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.

PubMed: 20796028
DOI: 10.1111/J.1742-4658.2010.07784.X

Experimental method

X-RAY DIFFRACTION (2.8 Å)