2i4l: Difference between revisions
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==Rhodopseudomonas palustris prolyl-tRNA synthetase== | ==Rhodopseudomonas palustris prolyl-tRNA synthetase== | ||
<StructureSection load='2i4l' size='340' side='right' caption='[[2i4l]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2i4l' size='340' side='right'caption='[[2i4l]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2i4l]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2i4l]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"rhodobacillus_palustris"_molisch_1907 "rhodobacillus palustris" molisch 1907]. 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> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">proS,RPA2928 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">proS,RPA2928 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1076 "Rhodobacillus palustris" Molisch 1907])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[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] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 31: | Line 31: | ||
==See Also== | ==See Also== | ||
*[[Aminoacyl tRNA | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Rhodobacillus palustris molisch 1907]] | [[Category: Rhodobacillus palustris molisch 1907]] | ||
[[Category: Large Structures]] | |||
[[Category: Proline--tRNA ligase]] | [[Category: Proline--tRNA ligase]] | ||
[[Category: Crepin, T]] | [[Category: Crepin, T]] | ||
Revision as of 10:27, 24 March 2021
Rhodopseudomonas palustris prolyl-tRNA synthetaseRhodopseudomonas palustris prolyl-tRNA synthetase
Structural highlights
Function[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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProlyl-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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