6I52

Yeast RPA bound to ssDNA

Summary for 6I52

• Entry DOI: 10.2210/pdb6i52/pdb
• EMDB information: 4410
• Descriptor: Replication factor A protein 3, Replication factor A protein 2, Replication factor A protein 1, ... (4 entities in total)
• Functional Keywords: complex, heterotrimer, dna binding, ob-fold, dna binding protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c); More
• Total number of polymer chains: 4
• Total formula weight: 55319.56

Authors

Yates, L.A.,Aramayo, R.J.,Zhang, X. (deposition date: 2018-11-12, release date: 2018-12-19, Last modification date: 2024-05-15)

Primary citation

Yates, L.A.,Aramayo, R.J.,Pokhrel, N.,Caldwell, C.C.,Kaplan, J.A.,Perera, R.L.,Spies, M.,Antony, E.,Zhang, X.
A structural and dynamic model for the assembly of Replication Protein A on single-stranded DNA.
Nat Commun, 9:5447-5447, 2018

PubMed Abstract: Replication Protein A (RPA), the major eukaryotic single stranded DNA-binding protein, binds to exposed ssDNA to protect it from nucleases, participates in a myriad of nucleic acid transactions and coordinates the recruitment of other important players. RPA is a heterotrimer and coats long stretches of single-stranded DNA (ssDNA). The precise molecular architecture of the RPA subunits and its DNA binding domains (DBDs) during assembly is poorly understood. Using cryo electron microscopy we obtained a 3D reconstruction of the RPA trimerisation core bound with ssDNA (∼55 kDa) at ∼4.7 Å resolution and a dimeric RPA assembly on ssDNA. FRET-based solution studies reveal dynamic rearrangements of DBDs during coordinated RPA binding and this activity is regulated by phosphorylation at S178 in RPA70. We present a structural model on how dynamic DBDs promote the cooperative assembly of multiple RPAs on long ssDNA.

PubMed: 30575763
DOI: 10.1038/s41467-018-07883-7

Experimental method

ELECTRON MICROSCOPY (4.7 Å)