2i4l
From Proteopedia
(New page: 200px<br /><applet load="2i4l" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i4l, resolution 2.00Å" /> '''Rhodopseudomonas pal...) |
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| - | [[Image:2i4l.jpg|left|200px]]<br /><applet load="2i4l" size=" | + | [[Image:2i4l.jpg|left|200px]]<br /><applet load="2i4l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2i4l, resolution 2.00Å" /> | caption="2i4l, resolution 2.00Å" /> | ||
'''Rhodopseudomonas palustris prolyl-tRNA synthetase'''<br /> | '''Rhodopseudomonas palustris prolyl-tRNA synthetase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Prolyl-tRNA synthetases (ProRSs) are unique among synthetases in that they | + | 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== | ==About this Structure== | ||
| - | 2I4L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris]. Active as [http://en.wikipedia.org/wiki/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] Full crystallographic information is available from [http:// | + | 2I4L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris]. Active as [http://en.wikipedia.org/wiki/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I4L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: alpha beta]] | [[Category: alpha beta]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:48:57 2008'' |
Revision as of 15:48, 21 February 2008
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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
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