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Flexibility and com...
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Ingvarsson, Henrik,1975-Uppsala universitet,Strukturell molekylärbiologi
(författare)
Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase
- Artikel/kapitelEngelska2010
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2010-08-26
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Wiley,2010
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LIBRIS-ID:oai:DiVA.org:uu-121752
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https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-121752URI
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https://doi.org/10.1111/j.1742-4658.2010.07784.xDOI
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Språk:engelska
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Sammanfattning på:engelska
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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.
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Unge, Torsten,1945-Uppsala universitet,Strukturell molekylärbiologi(Swepub:uu)torsunge
(författare)
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Uppsala universitetStrukturell molekylärbiologi
(creator_code:org_t)
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Ingår i:The FEBS Journal: Wiley277:19, s. 3947-39621742-464X1742-4658
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