4GOP

Structure and Conformational Change of a Replication Protein A Heterotrimer Bound to ssDNA

Summary for 4GOP

• Entry DOI: 10.2210/pdb4gop/pdb
• Descriptor: Putative uncharacterized protein, DNA (25-MER), ZINC ION, ... (5 entities in total)
• Functional Keywords: ob fold, ssdna binding, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Ustilago maydis (Smut fungus); More
• Total number of polymer chains: 8
• Total formula weight: 174031.82

Authors

Pavletich, N.P.,Jie, F. (deposition date: 2012-08-20, release date: 2012-11-28, Last modification date: 2024-11-06)

Primary citation

Fan, J.,Pavletich, N.P.
Structure and conformational change of a replication protein A heterotrimer bound to ssDNA.
Genes Dev., 26:2337-2347, 2012

PubMed Abstract: Replication protein A (RPA) is the main eukaryotic ssDNA-binding protein with essential roles in DNA replication, recombination, and repair. RPA maintains the DNA as single-stranded and also interacts with other DNA-processing proteins, coordinating their assembly and disassembly on DNA. RPA binds to ssDNA in two conformational states with opposing affinities for DNA and proteins. The RPA-protein interactions are compatible with a low DNA affinity state that involves DNA-binding domain A (DBD-A) and DBD-B but not with the high DNA affinity state that additionally engages DBD-C and DBD-D. The structure of the high-affinity RPA-ssDNA complex reported here shows a compact quaternary structure held together by a four-way interface between DBD-B, DBD-C, the intervening linker (BC linker), and ssDNA. The BC linker binds into the DNA-binding groove of DBD-B, mimicking DNA. The associated conformational change and partial occlusion of the DBD-A-DBA-B protein-protein interaction site establish a mechanism for the allosteric coupling of RPA-DNA and RPA-protein interactions.

PubMed: 23070815
DOI: 10.1101/gad.194787.112

Experimental method

X-RAY DIFFRACTION (3.1 Å)