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| {{STRUCTURE_2i4m| PDB=2i4m | SCENE= }} | | {{STRUCTURE_2i4m| PDB=2i4m | SCENE= }} |
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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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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17027500}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17027500 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17027500}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Yaremchuk, A.]] | | [[Category: Yaremchuk, A.]] |
| [[Category: Alpha beta]] | | [[Category: Alpha beta]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:03:41 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:37:15 2008'' |