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Flexibility and com...
Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase
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- Ingvarsson, Henrik, 1975- (author)
- Uppsala universitet,Strukturell molekylärbiologi
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- Unge, Torsten, 1945- (author)
- Uppsala universitet,Strukturell molekylärbiologi
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(creator_code:org_t)
- 2010-08-26
- 2010
- English.
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In: The FEBS Journal. - : Wiley. - 1742-464X .- 1742-4658. ; 277:19, s. 3947-3962
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Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Mycobacterium smegmatis
- methinoly-tRNA synthetase
- methionine
- adenosine
- Cell and molecular biology
- Cell- och molekylärbiologi
- Biologi med inriktning mot strukturbiologi
- Biology with specialization in Structural Biology
Publication and Content Type
- ref (subject category)
- art (subject category)
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