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methionyl-tRNA Synthetase (methionyl-trna + synthetase)

Distribution by Scientific Domains

Chemistry	100%

Selected Abstracts

Crystallization of Mycobacterium smegmatis methionyl-tRNA synthetase in the presence of methionine and adenosine

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 6 2009
Henrik Ingvarsson
Methionyl-tRNA synthetase (MetRS) from Mycobacterium smegmatis was recombinantly expressed in Escherichia coli and purified using Ni2+ -affinity and size-exclusion chromatography. Crystals formed readily in the presence of the ligands methionine and adenosine. These two ligands are components of an intermediate in the two-step catalytic mechanism of MetRS. The crystals were produced using the vapour-diffusion method and a full data set to 2.1,Å resolution was collected from a single crystal. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 155.9, b = 138.9, c = 123.3,Å, , = 124.8°. The presence of three molecules in the asymmetric unit corresponded to a solvent content of 60% and a Matthews coefficient of 3.1,Å3,Da,1. Structure determination is in progress. [source]

Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase

FEBS JOURNAL, Issue 19 2010
Henrik Ingvarsson
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. [source]

Modeling zinc sulfhydryl bonds in zinc fingers

INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY, Issue 3-4 2001
Johan Bredenberg
Abstract Molecular dynamics simulations have been carried out employing three different model descriptions of the zinc sulfhydryl interactions in class II fingers. One bonded and two nonbonded models were studied. Two variant structures of the glucocorticoid receptor DNA-binding domain and a NMR structure from a fragment of methionyl-tRNA synthetase were subjected to long-time MD simulations with these models. Our analysis is focused on comparison with experimental and quantum mechanical data, concerning the local Zn-finger and overall structural and dynamic properties for these models. All models performed well, but the nonbonded models appeared to reproduce the protein dynamics in better agreement with experimental data than does the bonded description. © 2001 John Wiley & Sons, Inc. Int J Quant Chem 83: 230,244, 2001 [source]