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==Crystal structure of Proteinaceous RNase P (PRORP) from Thermococcus celer== | ==Crystal structure of Proteinaceous RNase P (PRORP) from Thermococcus celer== | ||
<StructureSection load='7e8j' size='340' side='right'caption='[[7e8j]]' scene=''> | <StructureSection load='7e8j' size='340' side='right'caption='[[7e8j]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E8J FirstGlance]. <br> | <table><tr><td colspan='2'>[[7e8j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_celer_Vu_13_=_JCM_8558 Thermococcus celer Vu 13 = JCM 8558]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E8J FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7e8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e8j OCA], [https://pdbe.org/7e8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e8j RCSB], [https://www.ebi.ac.uk/pdbsum/7e8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e8j ProSAT]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7e8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e8j OCA], [https://pdbe.org/7e8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e8j RCSB], [https://www.ebi.ac.uk/pdbsum/7e8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e8j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/A0A218P4J1_THECE A0A218P4J1_THECE]] RNA-free RNase P that catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus.[HAMAP-Rule:MF_01078] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Besides the canonical RNA-based RNase P, pre-tRNA 5'-end processing can also be catalyzed by protein-only RNase P (PRORP). To date, various PRORPs have been discovered, but the basis underlying substrate binding and cleavage by HARPs (homolog of Aquifex RNase P) remains elusive. Here, we report structural and biochemical studies of HARPs. Comparison of the apo- and pre-tRNA-complexed structures showed that HARP is able to undergo large conformational changes that facilitate pre-tRNA binding and catalytic site formation. Planctomycetes bacterium HARP exists as dimer in vitro, but gel filtration and electron microscopy analysis confirmed that HARPs from Thermococcus celer, Thermocrinis minervae and Thermocrinis ruber can assemble into larger oligomers. Structural analysis, mutagenesis and in vitro biochemical studies all supported one cooperative pre-tRNA processing mode, in which one HARP dimer binds pre-tRNA at the elbow region whereas 5'-end removal is catalyzed by the partner dimer. Our studies significantly advance our understanding on pre-tRNA processing by PRORPs. | |||
Crystal structures and insights into precursor tRNA 5'-end processing by prokaryotic minimal protein-only RNase P.,Li Y, Su S, Gao Y, Lu G, Liu H, Chen X, Shao Z, Zhang Y, Shao Q, Zhao X, Yang J, Cao C, Lin J, Ma J, Gan J Nat Commun. 2022 Apr 28;13(1):2290. doi: 10.1038/s41467-022-30072-6. PMID:35484139<ref>PMID:35484139</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7e8j" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Thermococcus celer Vu 13 = JCM 8558]] | |||
[[Category: Gan JH]] | [[Category: Gan JH]] | ||
[[Category: Li YY]] | [[Category: Li YY]] | ||
Revision as of 10:01, 14 September 2022
Crystal structure of Proteinaceous RNase P (PRORP) from Thermococcus celerCrystal structure of Proteinaceous RNase P (PRORP) from Thermococcus celer
Structural highlights
Function[A0A218P4J1_THECE] RNA-free RNase P that catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus.[HAMAP-Rule:MF_01078] Publication Abstract from PubMedBesides the canonical RNA-based RNase P, pre-tRNA 5'-end processing can also be catalyzed by protein-only RNase P (PRORP). To date, various PRORPs have been discovered, but the basis underlying substrate binding and cleavage by HARPs (homolog of Aquifex RNase P) remains elusive. Here, we report structural and biochemical studies of HARPs. Comparison of the apo- and pre-tRNA-complexed structures showed that HARP is able to undergo large conformational changes that facilitate pre-tRNA binding and catalytic site formation. Planctomycetes bacterium HARP exists as dimer in vitro, but gel filtration and electron microscopy analysis confirmed that HARPs from Thermococcus celer, Thermocrinis minervae and Thermocrinis ruber can assemble into larger oligomers. Structural analysis, mutagenesis and in vitro biochemical studies all supported one cooperative pre-tRNA processing mode, in which one HARP dimer binds pre-tRNA at the elbow region whereas 5'-end removal is catalyzed by the partner dimer. Our studies significantly advance our understanding on pre-tRNA processing by PRORPs. Crystal structures and insights into precursor tRNA 5'-end processing by prokaryotic minimal protein-only RNase P.,Li Y, Su S, Gao Y, Lu G, Liu H, Chen X, Shao Z, Zhang Y, Shao Q, Zhao X, Yang J, Cao C, Lin J, Ma J, Gan J Nat Commun. 2022 Apr 28;13(1):2290. doi: 10.1038/s41467-022-30072-6. PMID:35484139[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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