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 PubMed
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).
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 Also
References
- ↑ Nakanishi K, Ogiso Y, Nakama T, Fukai S, Nureki O. Structural basis for anticodon recognition by methionyl-tRNA synthetase. Nat Struct Mol Biol. 2005 Oct;12(10):931-2. Epub 2005 Sep 11. PMID:16155581 doi:10.1038/nsmb988
