2ct8
Crystal structure of Aquifex aeolicus methionyl-tRNA synthetase complexed with tRNA(Met) and methionyl-adenylate anologueCrystal structure of Aquifex aeolicus methionyl-tRNA synthetase complexed with tRNA(Met) and methionyl-adenylate anologue
Structural highlights
Function[SYM_AQUAE] Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation (By similarity). Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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). Structural basis for anticodon recognition by methionyl-tRNA synthetase.,Nakanishi K, Ogiso Y, Nakama T, Fukai S, Nureki O Nat Struct Mol Biol. 2005 Oct;12(10):931-2. Epub 2005 Sep 11. PMID:16155581[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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