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. 2024 Jul 11;52(19):11626–11640. doi: 10.1093/nar/gkae584

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© The Author(s) 2024. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 1. — Architecture of the replication protein A (RPA) – ssDNA complex. (A) The three subunits of RPA—RPA70, RPA32 and RPA14 house several oligonucleotide/oligosaccharide binding (OB) domains that are classified as either DNA binding domains (DBDs: DBD-A, DBD-B, DBD-C and DBD-D) or protein-interaction domains (OB-F/PID^70N and winged helix (wh)/PID^32C). A structural model of RPA is shown and was generated using information from known structures of the OB-domains and AlphaFold2 models of the linkers. (B) Crystal structure of Ustilago maydis RPA bound to ssDNA is shown (PDB 4GNX). This structure lacks OB-F, the F-A linker, wh and the D-wh linker. ssDNA from CryoEM structures of Saccharomyces cerevisiae RPA (PDB 6I52) and Pyrococcus abyssi RPA (8OEL) are superimposed and reveal an end-to-end DNA distance of ∼55 Å. Structural data supports partial wrapping of ssDNA around the OB domains.