6lw3

Crystal structure of RuvC from Pseudomonas aeruginosaCrystal structure of RuvC from Pseudomonas aeruginosa

Structural highlights 6lw3 is a 2 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: 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 ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885) Activity: Crossover junction endodeoxyribonuclease, with EC number 3.1.22.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Resolvase 3D structures

spinqualitylabelsall models 6lw3, resolution 2.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image