PDBsum entry 4d6p

Hydrolase

PDB id: 4d6p

Contents

Protein chains

226 a.a.

Ligands

ANP ×2

GOL ×2

Metals

_MG ×2

Waters ×598

PDB id:

4d6p

Name:

Hydrolase

Title:

Rada c-terminal atpase domain from pyrococcus furiosus bound to amppnp

Structure:

DNA repair and recombination protein rada. Chain: a, b. Fragment: c-terminal atpase domain, unp residues 108-349. Synonym: rada. Engineered: yes. Mutation: yes

Source:

Pyrococcus furiosus. Organism_taxid: 2261. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.48Å R-factor: 0.193 R-free: 0.239

Authors:

M.E.Marsh,M.T.Ehebauer,D.Scott,C.Abell,T.L.Blundell,M.Hyvonen

Key ref:

M.E.Marsh et al. (2016). ATP half-sites in RadA and RAD51 recombinases bind nucleotides. Febs Open Bio, 6, 372-385. PubMed id: 27419043 DOI: 10.1002/2211-5463.12052

Date:

13-Nov-14 Release date: 14-Jan-15

Supersedes:

4a74

Protein chains

O74036  (RADA_PYRFU) -  DNA repair and recombination protein RadA from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Seq: 349 a.a.

Struc: 226 a.a.

DOI no: 10.1002/2211-5463.12052

Febs Open Bio 6:372-385 (2016)

PubMed id: 27419043

ATP half-sites in RadA and RAD51 recombinases bind nucleotides.

M.E.Marsh, D.E.Scott, M.T.Ehebauer, C.Abell, T.L.Blundell, M.Hyvönen.

ABSTRACT

Homologous recombination is essential for repair of DNA double-strand breaks. Central to this process is a family of recombinases, including archeal RadA and human RAD51, which form nucleoprotein filaments on damaged single-stranded DNA ends and facilitate their ATP-dependent repair. ATP binding and hydrolysis are dependent on the formation of a nucleoprotein filament comprising RadA/RAD51 and single-stranded DNA, with ATP bound between adjacent protomers. We demonstrate that truncated, monomeric Pyrococcus furiosus RadA and monomerised human RAD51 retain the ability to bind ATP and other nucleotides with high affinity. We present crystal structures of both apo and nucleotide-bound forms of monomeric RadA. These structures reveal that while phosphate groups are tightly bound, RadA presents a shallow, poorly defined binding surface for the nitrogenous bases of nucleotides. We suggest that RadA monomers would be constitutively bound to nucleotides in the cell and that the bound nucleotide might play a structural role in filament assembly.