2i4l

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[[Image:2i4l.jpg|left|200px]]
[[Image:2i4l.jpg|left|200px]]
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{{Structure
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|PDB= 2i4l |SIZE=350|CAPTION= <scene name='initialview01'>2i4l</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_2i4l", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE= proS,RPA2928 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1076 Rhodopseudomonas palustris])
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|DOMAIN=
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{{STRUCTURE_2i4l| PDB=2i4l | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i4l OCA], [http://www.ebi.ac.uk/pdbsum/2i4l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i4l RCSB]</span>
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'''Rhodopseudomonas palustris prolyl-tRNA synthetase'''
'''Rhodopseudomonas palustris prolyl-tRNA synthetase'''
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[[Category: Tukalo, M.]]
[[Category: Tukalo, M.]]
[[Category: Yaremchuk, A.]]
[[Category: Yaremchuk, A.]]
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[[Category: alpha beta]]
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[[Category: Alpha beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:03:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:39:33 2008''
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Revision as of 04:03, 4 May 2008

Template:STRUCTURE 2i4l

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. 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 Page seeded by OCA on Sun May 4 07:03:41 2008

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