PDBsum entry 4uqo

Hydrolase

PDB id: 4uqo

Contents

Protein chains

222 a.a.

Ligands

ADP ×2

Metals

_NA ×3

_MG ×2

Waters ×496

References listed in PDB file

Key reference

• Title: Atp half-Sites in rada and rad51 recombinases bind nucleotides.
• Authors: M.E.Marsh, D.E.Scott, M.T.Ehebauer, C.Abell, T.L.Blundell, M.Hyvönen.
• Ref.: Febs Open Bio, 2016, 6, 372-385. [DOI no: 10.1002/2211-5463.12052]
• PubMed id: 27419043

Note: In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above have been manually determined.

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.