4b2p

RadA C-terminal ATPase domain from Pyrococcus furiosus bound to GTP

spinqualitylabelsall models 4b2p, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4b2p is a 1 chain structure with sequence from Atcc 43587. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, GTP, MG Related: 1pzn, 4a6p, 4a6x, 4a74, 4a7o, 4b2i, 4b2l Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RADA_PYRFU] Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules. Publication Abstract from PubMed 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. ATP half-sites in RadA and RAD51 recombinases bind nucleotides.,Marsh ME, Scott DE, Ehebauer MT, Abell C, Blundell TL, Hyvonen M FEBS Open Bio. 2016 Apr 6;6(5):372-85. doi: 10.1002/2211-5463.12052. eCollection , 2016 May. PMID:27419043 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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