2j3m: Difference between revisions
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Revision as of 18:18, 30 October 2007
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PROLYL-TRNA SYNTHETASE FROM ENTEROCOCCUS FAECALIS COMPLEXED WITH ATP, MANGANESE AND PROLINOL
OverviewOverview
Prolyl-tRNA synthetases (ProRSs) are unique among synthetases in that they, have diverse architectures, notably the variable presence of a cis-editing, domain homologous to the freestanding deacylase proteins YbaK and ProX., Here, we describe crystal structures of two bacterial ProRSs from the, pathogen Enterococcus faecalis, which possesses an editing domain, and, from Rhodopseudomonas palustris, which does not. We compare the overall, structure and binding mode of ATP and prolyl-adenylate with those of the, archael/eukaryote-type ProRS from Thermus thermophilus. Although, structurally more homologous to YbaK, which preferentially hydrolyzes, Cys-tRNA(Pro), the editing domain of E. faecalis ProRS possesses key, elements similar to ProX, with which it shares the activity of hydrolyzing, ... [(full description)]
About this StructureAbout this Structure
2J3M is a [Single protein] structure of sequence from [Enterococcus faecalis] with MN, ATP and PRI as [ligands]. Active as [Proline--tRNA ligase], with EC number [6.1.1.15]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structures of two bacterial prolyl-tRNA synthetases with and without a cis-editing domain., Crepin T, Yaremchuk A, Tukalo M, Cusack S, Structure. 2006 Oct;14(10):1511-25. PMID:17027500
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