1HQC

STRUCTURE OF RUVB FROM THERMUS THERMOPHILUS HB8

Summary for 1HQC

• Entry DOI: 10.2210/pdb1hqc/pdb
• Descriptor: RUVB, MAGNESIUM ION, ADENINE (3 entities in total)
• Functional Keywords: extended aaa-atpase domain, ruvb, complex with nucleotide, hydrolase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 72420.31

Authors

Yamada, K.,Kunishima, N.,Mayanagi, K.,Iwasaki, H.,Morikawa, K. (deposition date: 2000-12-15, release date: 2001-02-21, Last modification date: 2024-03-13)

Primary citation

Yamada, K.,Kunishima, N.,Mayanagi, K.,Ohnishi, T.,Nishino, T.,Iwasaki, H.,Shinagawa, H.,Morikawa, K.
Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8.
Proc.Natl.Acad.Sci.USA, 98:1442-1447, 2001

PubMed Abstract: We report here the crystal structure of the RuvB motor protein from Thermus thermophilus HB8, which drives branch migration of the Holliday junction during homologous recombination. RuvB has a crescent-like architecture consisting of three consecutive domains, the first two of which are involved in ATP binding and hydrolysis. DNA is likely to interact with a large basic cleft, which encompasses the ATP-binding pocket and domain boundaries, whereas the junction-recognition protein RuvA may bind a flexible beta-hairpin protruding from the N-terminal domain. The structures of two subunits, related by a noncrystallographic pseudo-2-fold axis, imply that conformational changes of motor protein coupled with ATP hydrolysis may reflect motility essential for its translocation around double-stranded DNA.

PubMed: 11171970
DOI: 10.1073/pnas.031470598

Experimental method

X-RAY DIFFRACTION (3.2 Å)