1ixs

Structure of RuvB complexed with RuvA domain III

spinqualitylabelsall models 1ixs, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ixs is a 2 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANP Related: 1hqc, 1ixr Gene: ruva (Thermus thermophilus), ruvb (Thermus thermophilus) Activity: Adenosinetriphosphatase, with EC number 3.6.1.3 Resources: FirstGlance, OCA, RCSB, PDBsum Function [RUVA_THET8] The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB (By similarity). [RUVB_THET8] The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvB is a Mg(2+)-dependent, DNA-dependent ATPase with an equal preference for supercoiled and linear duplex DNA. It can promote Holliday junction migration alone. 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 PubMed We present the X-ray structure of the RuvA-RuvB complex, which plays a crucial role in ATP-dependent branch migration. Two RuvA tetramers form the symmetric and closed octameric shell, where four RuvA domain IIIs spring out in the two opposite directions to be individually caught by a single RuvB. The binding of domain III deforms the protruding beta hairpin in the N-terminal domain of RuvB and thereby appears to induce a functional and less symmetric RuvB hexameric ring. The model of the RuvA-RuvB junction DNA ternary complex, constructed by fitting the X-ray structure into the averaged electron microscopic images of the RuvA-RuvB junction, appears to be more compatible with the branch migration mode of a fixed RuvA-RuvB interaction than with a rotational interaction mode. Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery.,Yamada K, Miyata T, Tsuchiya D, Oyama T, Fujiwara Y, Ohnishi T, Iwasaki H, Shinagawa H, Ariyoshi M, Mayanagi K, Morikawa K Mol Cell. 2002 Sep;10(3):671-81. PMID:12408833 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Helicase

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