1IN7

THERMOTOGA MARITIMA RUVB R170A

Summary for 1IN7

• Entry DOI: 10.2210/pdb1in7/pdb
• Related: 1IN4 1IN5 1IN6 1IN8 1J7K
• Descriptor: HOLLIDAY JUNCTION DNA HELICASE RUVB, ACETATE ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: aaa+-class atpase, winged-helix domain, holliday junction, branch migration, dna translocase, walker a, walker b, sensor 1, sensor 2, arginine finger, dna binding protein
• Biological source: Thermotoga maritima
• Total number of polymer chains: 1
• Total formula weight: 37665.35

Authors

Putnam, C.D.,Clancy, S.B.,Tsuruta, H.,Wetmur, J.G.,Tainer, J.A. (deposition date: 2001-05-12, release date: 2001-08-08, Last modification date: 2023-08-16)

Primary citation

Putnam, C.D.,Clancy, S.B.,Tsuruta, H.,Gonzalez, S.,Wetmur, J.G.,Tainer, J.A.
Structure and mechanism of the RuvB Holliday junction branch migration motor.
J.Mol.Biol., 311:297-310, 2001

PubMed Abstract: The RuvB hexamer is the chemomechanical motor of the RuvAB complex that migrates Holliday junction branch-points in DNA recombination and the rescue of stalled DNA replication forks. The 1.6 A crystal structure of Thermotoga maritima RuvB together with five mutant structures reveal that RuvB is an ATPase-associated with diverse cellular activities (AAA+-class ATPase) with a winged-helix DNA-binding domain. The RuvB-ADP complex structure and mutagenesis suggest how AAA+-class ATPases couple nucleotide binding and hydrolysis to interdomain conformational changes and asymmetry within the RuvB hexamer implied by the crystallographic packing and small-angle X-ray scattering in solution. ATP-driven domain motion is positioned to move double-stranded DNA through the hexamer and drive conformational changes between subunits by altering the complementary hydrophilic protein- protein interfaces. Structural and biochemical analysis of five motifs in the protein suggest that ATP binding is a strained conformation recognized both by sensors and the Walker motifs and that intersubunit activation occurs by an arginine finger motif reminiscent of the GTPase-activating proteins. Taken together, these results provide insights into how RuvB functions as a motor for branch migration of Holliday junctions.

PubMed: 11478862
DOI: 10.1006/jmbi.2001.4852

Experimental method

X-RAY DIFFRACTION (1.9 Å)