2i4l

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(New page: 200px<br /><applet load="2i4l" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i4l, resolution 2.00&Aring;" /> '''Rhodopseudomonas pal...)
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[[Image:2i4l.jpg|left|200px]]<br /><applet load="2i4l" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2i4l, resolution 2.00&Aring;" />
 
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'''Rhodopseudomonas palustris prolyl-tRNA synthetase'''<br />
 
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==Overview==
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==Rhodopseudomonas palustris prolyl-tRNA synthetase==
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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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<StructureSection load='2i4l' size='340' side='right'caption='[[2i4l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2i4l]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I4L FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i4l OCA], [https://pdbe.org/2i4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i4l RCSB], [https://www.ebi.ac.uk/pdbsum/2i4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i4l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYP_RHOPA SYP_RHOPA] Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can inadvertently accommodate and process cysteine. The misacylated Cys-tRNA(Pro) is not edited by ProRS.[HAMAP-Rule:MF_01570]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i4/2i4l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2i4l ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2I4L OCA].
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17027500 17027500]
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[[Category: Large Structures]]
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[[Category: Proline--tRNA ligase]]
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[[Category: Rhodopseudomonas palustris]]
[[Category: Rhodopseudomonas palustris]]
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[[Category: Single protein]]
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[[Category: Crepin T]]
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[[Category: Crepin, T.]]
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[[Category: Cusack S]]
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[[Category: Cusack, S.]]
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[[Category: Tukalo M]]
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[[Category: Tukalo, M.]]
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[[Category: Yaremchuk A]]
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[[Category: Yaremchuk, A.]]
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[[Category: alpha beta]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:08:53 2007''
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Current revision

Rhodopseudomonas palustris prolyl-tRNA synthetase

PDB ID 2i4l

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