2x1m

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

spinqualitylabelsall models 2x1m, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2x1m is a 1 chain structure with sequence from Mycs2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 2HP, CXS, MET Related: 2x1l Activity: Methionine--tRNA ligase, with EC number 6.1.1.10 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0R3E2_MYCS2] Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation (By similarity).[SAAS:SAAS023457_004_015657][HAMAP-Rule:MF_01228] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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