9qmp
From Proteopedia
E.coli seryl-tRNA synthetase
Structural highlights
FunctionSYS_ECOLI Catalyzes the attachment of serine to tRNA(Ser) (PubMed:7537870). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).[1] [2] [3] Publication Abstract from PubMedThe three-dimensional crystal structure of seryl-transfer RNA synthetase from Escherichia coli, refined at 2.5 A resolution, is described. It has an N-terminal domain that forms an antiparallel alpha helical coiled-coil, stretching 60 A out into the solvent and stabilized by interhelical hydrophobic interactions and an active-site alpha-beta domain based around a seven-stranded antiparallel beta sheet. Unlike the three other known synthetase structures, the enzyme contains no classical nucleotide-binding fold, and is the first representative of a second class of aminoacyl-tRNA synthetase structures. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.,Cusack S, Berthet-Colominas C, Hartlein M, Nassar N, Leberman R Nature. 1990 Sep 20;347(6290):249-55. PMID:2205803[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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