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2j3l

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{{STRUCTURE_2j3l| PDB=2j3l | SCENE= }}
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'''PROLYL-TRNA SYNTHETASE FROM ENTEROCOCCUS FAECALIS COMPLEXED WITH A PROLYL-ADENYLATE ANALOGUE ('5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE)'''
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===PROLYL-TRNA SYNTHETASE FROM ENTEROCOCCUS FAECALIS COMPLEXED WITH A PROLYL-ADENYLATE ANALOGUE ('5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE)===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17027500 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17027500}}
==About this Structure==
==About this Structure==
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[[Category: Yaremchuk, A.]]
[[Category: Yaremchuk, A.]]
[[Category: Ligase]]
[[Category: Ligase]]
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Revision as of 13:24, 5 July 2008

Image:2j3l.png

Template:STRUCTURE 2j3l

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

Template:ABSTRACT PUBMED 17027500

About this Structure

2J3L is a Single protein structure of sequence from Enterococcus faecalis. 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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