2j3l

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[[Image:2j3l.gif|left|200px]]<br /><applet load="2j3l" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2j3l, resolution 2.30&Aring;" />
 
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'''PROLYL-TRNA SYNTHETASE FROM ENTEROCOCCUS FAECALIS COMPLEXED WITH A PROLYL-ADENYLATE ANALOGUE ('5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE)'''<br />
 
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==Overview==
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==Prolyl-tRNA synthetase from Enterococcus faecalis complexed with a prolyl-adenylate analogue ('5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE)==
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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='2j3l' size='340' side='right'caption='[[2j3l]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2j3l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J3L 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]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P5A:5-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE'>P5A</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2j3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j3l OCA], [https://pdbe.org/2j3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j3l RCSB], [https://www.ebi.ac.uk/pdbsum/2j3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j3l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYP_ENTFA SYP_ENTFA] 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.[HAMAP-Rule:MF_01569]
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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/j3/2j3l_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=2j3l 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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2J3L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=P5A:'>P5A</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Known structural/functional Site: <scene name='pdbsite=AC1:P5a+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J3L 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: Enterococcus faecalis]]
[[Category: Enterococcus faecalis]]
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[[Category: Proline--tRNA ligase]]
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[[Category: Large Structures]]
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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: P5A]]
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[[Category: SO4]]
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[[Category: atp + l-proline + trna (pro) gives amp + ppi + l-prolyl-trna(pro)]]
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[[Category: bacterial-type prolyl-trna synthetase]]
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[[Category: class ii aminoacyl-trna synthetase]]
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[[Category: editing]]
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[[Category: ligase]]
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[[Category: translation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:41:09 2008''
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Current revision

Prolyl-tRNA synthetase from Enterococcus faecalis complexed with a prolyl-adenylate analogue ('5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE)

PDB ID 2j3l

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