2i4m: Difference between revisions
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'''Rhodopseudomonas palustris prolyl-tRNA synthetase in complex with ProAMS''' | '''Rhodopseudomonas palustris prolyl-tRNA synthetase in complex with ProAMS''' | ||
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[[Category: Tukalo, M.]] | [[Category: Tukalo, M.]] | ||
[[Category: Yaremchuk, A.]] | [[Category: Yaremchuk, A.]] | ||
[[Category: | [[Category: Alpha beta]] | ||
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Revision as of 07:03, 4 May 2008
Rhodopseudomonas palustris prolyl-tRNA synthetase in complex with ProAMS
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 Ala-tRNA(Pro). The structures give insight into the complex evolution of ProRSs, the mechanism of editing, and structural differences between prokaryotic- and eukaryotic-type ProRSs that can be exploited for antibiotic design.
About this StructureAbout this Structure
2I4M is a Single protein structure of sequence from Rhodopseudomonas palustris. 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 Page seeded by OCA on Sun May 4 07:03:41 2008