Literature DB >> 16155581

Structural basis for anticodon recognition by methionyl-tRNA synthetase.

Kotaro Nakanishi1, Yuri Ogiso, Takashi Nakama, Shuya Fukai, Osamu Nureki.   

Abstract

In the 2.7-A resolution crystal structure of methionyl-tRNA synthetase (MetRS) in complex with tRNA(Met) and a methionyl-adenylate analog, the tRNA anticodon loop is distorted to form a triple-base stack comprising C34, A35 and A38. A tryptophan residue stacks on C34 to extend the triple-base stack. In addition, C34 forms Watson-Crick-type hydrogen bonds with Arg357. This structure resolves the longstanding question of how MetRS specifically recognizes tRNA(Met).

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Year:  2005        PMID: 16155581     DOI: 10.1038/nsmb988

Source DB:  PubMed          Journal:  Nat Struct Mol Biol        ISSN: 1545-9985            Impact factor:   15.369


  35 in total

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5.  Bringing order to translation: the contributions of transfer RNA anticodon-domain modifications.

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7.  Misacylation of specific nonmethionyl tRNAs by a bacterial methionyl-tRNA synthetase.

Authors:  Thomas E Jones; Rebecca W Alexander; Tao Pan
Journal:  Proc Natl Acad Sci U S A       Date:  2011-04-11       Impact factor: 11.205

8.  Biallelic Mutations of Methionyl-tRNA Synthetase Cause a Specific Type of Pulmonary Alveolar Proteinosis Prevalent on Réunion Island.

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Journal:  Am J Hum Genet       Date:  2015-04-23       Impact factor: 11.025

9.  Distinct states of methionyl-tRNA synthetase indicate inhibitor binding by conformational selection.

Authors:  Cho Yeow Koh; Jessica E Kim; Sayaka Shibata; Ranae M Ranade; Mingyan Yu; Jiyun Liu; J Robert Gillespie; Frederick S Buckner; Christophe L M J Verlinde; Erkang Fan; Wim G J Hol
Journal:  Structure       Date:  2012-08-16       Impact factor: 5.006

10.  Switching from an induced-fit to a lock-and-key mechanism in an aminoacyl-tRNA synthetase with modified specificity.

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Journal:  J Mol Biol       Date:  2009-10-23       Impact factor: 5.469

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