1u0b
Crystal structure of cysteinyl-tRNA synthetase binary complex with tRNACys
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OverviewOverview
The crystal structure of Escherichia coli cysteinyl-tRNA synthetase, (CysRS) bound to tRNA(Cys) at a resolution of 2.3 A reveals base-specific, and shape-selective interactions across an extensive protein-RNA, recognition interface. The complex contains a mixed alpha/beta C-terminal, domain, which is disordered in the unliganded enzyme. This domain makes, specific hydrogen bonding interactions with all three bases of the GCA, anticodon. The tRNA anticodon stem is bent sharply toward the enzyme as, compared with its conformation when bound to elongation factor Tu, providing an essential basis for shape-selective recognition. The CysRS, structure also reveals interactions of conserved enzyme groups with the, sugar-phosphate backbone in the D loop, adjacent to an unusual G15.G48, tertiary base pair previously implicated in tRNA aminoacylation. A, combined mutational analysis of enzyme and tRNA groups at G15.G48 supports, the notion that contacts between CysRS and the sugar-phosphate backbone, contribute to recognition by indirect readout.
About this StructureAbout this Structure
1U0B is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Active as Cysteine--tRNA ligase, with EC number 6.1.1.16 Full crystallographic information is available from OCA.
ReferenceReference
Shape-selective RNA recognition by cysteinyl-tRNA synthetase., Hauenstein S, Zhang CM, Hou YM, Perona JJ, Nat Struct Mol Biol. 2004 Nov;11(11):1134-41. Epub 2004 Oct 17. PMID:15489861
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