8FS3
Structure of S. cerevisiae Rad24-RFC loading the 9-1-1 clamp onto a 10-nt gapped DNA in step 1 (open 9-1-1 and shoulder bound DNA only)
Summary for 8FS3
| Entry DOI | 10.2210/pdb8fs3/pdb |
| EMDB information | 29412 |
| Descriptor | Checkpoint protein RAD24, Primer strand 2, MAGNESIUM ION, ... (13 entities in total) |
| Functional Keywords | dna damage repair, rad24-rfc, 9-1-1 clamp, dna clamp, alternative clamp loader, dna damage signaling, dna binding protein-dna complex, cell cycle-dna complex, cell cycle/dna |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 10 |
| Total formula weight | 409347.67 |
| Authors | Zheng, F.,Georgescu, R.,Yao, Y.N.,O'Donnell, M.E.,Li, H. (deposition date: 2023-01-09, release date: 2023-06-14, Last modification date: 2026-04-29) |
| Primary citation | Zheng, F.,Georgescu, R.E.,Yao, N.Y.,O'Donnell, M.E.,Li, H. Structures of 9-1-1 DNA checkpoint clamp loading at gaps from start to finish and ramification on biology. Cell Rep, 42:112694-112694, 2023 Cited by PubMed Abstract: Rad24-RFC (replication factor C) loads the 9-1-1 checkpoint clamp onto the recessed 5' ends by binding a 5' DNA at an external surface site and threading the 3' single-stranded DNA (ssDNA) into 9-1-1. We find here that Rad24-RFC loads 9-1-1 onto DNA gaps in preference to a recessed 5' end, thus presumably leaving 9-1-1 on duplex 3' ss/double-stranded DNA (dsDNA) after Rad24-RFC ejects from DNA. We captured five Rad24-RFC-9-1-1 loading intermediates using a 10-nt gap DNA. We also determined the structure of Rad24-RFC-9-1-1 using a 5-nt gap DNA. The structures reveal that Rad24-RFC is unable to melt DNA ends and that a Rad24 loop limits the dsDNA length in the chamber. These observations explain Rad24-RFC's preference for a preexisting gap of over 5-nt ssDNA and suggest a direct role of the 9-1-1 in gap repair with various TLS (trans-lesion synthesis) polymerases in addition to signaling the ATR kinase. PubMed: 37392384DOI: 10.1016/j.celrep.2023.112694 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.93 Å) |
Structure validation
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