1J7K
THERMOTOGA MARITIMA RUVB P216G MUTANT
Summary for 1J7K
| Entry DOI | 10.2210/pdb1j7k/pdb |
| Related | 1IN4 1IN5 1IN6 1IN7 1IN8 |
| Descriptor | HOLLIDAY JUNCTION DNA HELICASE RUVB, ACETATE ION, COBALT (II) ION, ... (6 entities in total) |
| Functional Keywords | aaa+-class atpase, winged-helix domain, dna translocase, holliday junction, branch migration, 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 | 37968.49 |
| Authors | Putnam, C.D.,Clancy, S.B.,Tsuruta, H.,Wetmur, J.G.,Tainer, J.A. (deposition date: 2001-05-16, 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 Cited by 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: 11478862DOI: 10.1006/jmbi.2001.4852 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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