6lw3: Difference between revisions
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<StructureSection load='6lw3' size='340' side='right'caption='[[6lw3]], [[Resolution|resolution]] 2.38Å' scene=''> | <StructureSection load='6lw3' size='340' side='right'caption='[[6lw3]], [[Resolution|resolution]] 2.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6lw3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LW3 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6lw3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LW3 FirstGlance]. <br> | ||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ruvC, C0044_06995, CAZ10_11430, CGU42_02205, CKA47_33020, DY930_19340, DZ934_18445, DZ962_02435, E4V10_33000, EQH76_21345, FCG96_31605, FLI88_33360, IPC1481_05880, IPC1482_18775, IPC165_11875, IPC170_03130, IPC47_08385, IPC669_29490, RW109_RW109_05217 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</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/Crossover_junction_endodeoxyribonuclease Crossover junction endodeoxyribonuclease], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.22.4 3.1.22.4] </span></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=6lw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lw3 OCA], [https://pdbe.org/6lw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lw3 RCSB], [https://www.ebi.ac.uk/pdbsum/6lw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lw3 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/A0A0C7D4E1_PSEAI A0A0C7D4E1_PSEAI]] Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.[HAMAP-Rule:MF_00034][SAAS:SAAS01093222] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Holliday junction, a four-way DNA structure, is an important intermediate of homologous recombination. Proper Holliday junction resolution is critical to complete the recombination process. In most bacterial cells, the Holliday junction cleavage is mainly performed by a specific endonuclease RuvC. Here, we describe the biochemical properties and the crystal structure of RuvC from an opportunistic pathogen, Pseudomonas aeruginosa (PaRuvC). PaRuvC specifically binds to the Holliday junction DNA and preferentially cleaves it at the consensus 5'-TTC-3'. PaRuvC uses Mg(2+) as the preferred divalent metal cofactor for Holliday junction cleavage and its optimum pH is 8.0-9.0. Elevated temperatures (37-60 degrees C) boost the catalytic activity, but temperatures higher than 53 degrees C reduce the protein stability. The crystal structure of PaRuvC determined at 2.4 A and mutagenesis analysis reveal key residues involved in the dimer formation, substrate binding and catalysis. Our results are expected to provide useful information to combat antibiotic resistance of Pseudomonas aeruginosa by targeting its homologous recombination system. | |||
Biochemical and structural characterization of the Holliday junction resolvase RuvC from Pseudomonas aeruginosa.,Hu Y, He Y, Lin Z Biochem Biophys Res Commun. 2020 Apr 30;525(2):265-271. doi:, 10.1016/j.bbrc.2020.02.062. Epub 2020 Feb 19. PMID:32085896<ref>PMID:32085896</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6lw3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Resolvase 3D structures|Resolvase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:44, 16 February 2022
Crystal structure of RuvC from Pseudomonas aeruginosaCrystal structure of RuvC from Pseudomonas aeruginosa
Structural highlights
Function[A0A0C7D4E1_PSEAI] Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.[HAMAP-Rule:MF_00034][SAAS:SAAS01093222] Publication Abstract from PubMedThe Holliday junction, a four-way DNA structure, is an important intermediate of homologous recombination. Proper Holliday junction resolution is critical to complete the recombination process. In most bacterial cells, the Holliday junction cleavage is mainly performed by a specific endonuclease RuvC. Here, we describe the biochemical properties and the crystal structure of RuvC from an opportunistic pathogen, Pseudomonas aeruginosa (PaRuvC). PaRuvC specifically binds to the Holliday junction DNA and preferentially cleaves it at the consensus 5'-TTC-3'. PaRuvC uses Mg(2+) as the preferred divalent metal cofactor for Holliday junction cleavage and its optimum pH is 8.0-9.0. Elevated temperatures (37-60 degrees C) boost the catalytic activity, but temperatures higher than 53 degrees C reduce the protein stability. The crystal structure of PaRuvC determined at 2.4 A and mutagenesis analysis reveal key residues involved in the dimer formation, substrate binding and catalysis. Our results are expected to provide useful information to combat antibiotic resistance of Pseudomonas aeruginosa by targeting its homologous recombination system. Biochemical and structural characterization of the Holliday junction resolvase RuvC from Pseudomonas aeruginosa.,Hu Y, He Y, Lin Z Biochem Biophys Res Commun. 2020 Apr 30;525(2):265-271. doi:, 10.1016/j.bbrc.2020.02.062. Epub 2020 Feb 19. PMID:32085896[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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