PDBsum entry 2zuc

Recombination

PDB id: 2zuc

Contents

Protein chains

297 a.a. *

Waters ×12

* Residue conservation analysis

PDB id:

2zuc

Name:

Recombination

Title:

Crystal structure of left-handed rada filament

Structure:

DNA repair and recombination protein rada. Chain: a, b. Engineered: yes

Source:

Sulfolobus solfataricus. Organism_taxid: 2287. Gene: rada. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.30Å R-factor: 0.228 R-free: 0.283

Authors:

Y.W.Chang,T.P.Ko,T.F.Wang,A.H.J.Wang

Key ref:

Y.W.Chang et al. (2009). Three new structures of left-handed RADA helical filaments: structural flexibility of N-terminal domain is critical for recombinase activity. Plos One, 4, e4890. PubMed id: 19295907

Date:

15-Oct-08 Release date: 07-Apr-09

Protein chains

Q55075  (RADA_SULSO) -  DNA repair and recombination protein RadA from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

Seq: 324 a.a.

Struc: 297 a.a.

Plos One 4:e4890 (2009)

PubMed id: 19295907

Three new structures of left-handed RADA helical filaments: structural flexibility of N-terminal domain is critical for recombinase activity.

Y.W.Chang, T.P.Ko, C.D.Lee, Y.C.Chang, K.A.Lin, C.S.Chang, A.H.Wang, T.F.Wang.

ABSTRACT

RecA family proteins, including bacterial RecA, archaeal RadA, and eukaryotic Dmc1 and Rad51, mediate homologous recombination, a reaction essential for maintaining genome integrity. In the presence of ATP, these proteins bind a single-strand DNA to form a right-handed nucleoprotein filament, which catalyzes pairing and strand exchange with a homologous double-stranded DNA (dsDNA), by as-yet unknown mechanisms. We recently reported a structure of RadA left-handed helical filament, and here present three new structures of RadA left-handed helical filaments. Comparative structural analysis between different RadA/Rad51 helical filaments reveals that the N-terminal domain (NTD) of RadA/Rad51, implicated in dsDNA binding, is highly flexible. We identify a hinge region between NTD and polymerization motif as responsible for rigid body movement of NTD. Mutant analysis further confirms that structural flexibility of NTD is essential for RadA's recombinase activity. These results support our previous hypothesis that ATP-dependent axial rotation of RadA nucleoprotein helical filament promotes homologous recombination.