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1.	Ingvarsson, Henrik, 1975-, et al. (författare) Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase 2010 Ingår i: The FEBS Journal. - : Wiley. - 1742-464X .- 1742-4658. ; 277:19, s. 3947-3962 Tidskriftsartikel (refereegranskat)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.

Ingvarsson, Henrik, 1975-, et al. (författare)
Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase
2010
Ingår i: The FEBS Journal. - : Wiley. - 1742-464X .- 1742-4658. ; 277:19, s. 3947-3962
Tidskriftsartikel (refereegranskat)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.

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