2I4L

Rhodopseudomonas palustris prolyl-tRNA synthetase

Summary for 2I4L

• Entry DOI: 10.2210/pdb2i4l/pdb
• Descriptor: Proline-tRNA ligase (2 entities in total)
• Functional Keywords: alpha beta, ligase
• Biological source: Rhodopseudomonas palustris
• Cellular location: Cytoplasm: Q6N5P6
• Total number of polymer chains: 3
• Total formula weight: 154636.39

Authors

Crepin, T.,Yaremchuk, A.,Tukalo, M.,Cusack, S. (deposition date: 2006-08-22, release date: 2006-10-24, Last modification date: 2024-02-21)

Primary citation

Crepin, T.,Yaremchuk, A.,Tukalo, M.,Cusack, S.
Structures of Two Bacterial Prolyl-tRNA Synthetases with and without a cis-Editing Domain.
Structure, 14:1511-1525, 2006

PubMed Abstract: 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.

PubMed: 17027500
DOI: 10.1016/j.str.2006.08.007

Experimental method

X-RAY DIFFRACTION (2 Å)