2i4l
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="2i4l" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i4l, resolution 2.00Å" /> '''Rhodopseudomonas pal...)
Next diff →
Revision as of 10:01, 21 November 2007
|
Rhodopseudomonas palustris prolyl-tRNA synthetase
Overview
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 Structure
2I4L is a Single protein structure of sequence from Rhodopseudomonas palustris. Active as Proline--tRNA ligase, with EC number 6.1.1.15 Full crystallographic information is available from OCA.
Reference
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 Wed Nov 21 12:08:53 2007
