2j3l

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spinqualitylabelsall models 2j3l, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

PROLYL-TRNA SYNTHETASE FROM ENTEROCOCCUS FAECALIS COMPLEXED WITH A PROLYL-ADENYLATE ANALOGUE ('5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE)

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

2J3L is a Single protein structure of sequence from Enterococcus faecalis with SO4 and P5A as ligands. Active as Proline--tRNA ligase, with EC number 6.1.1.15 Known structural/functional Site: . 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

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