Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	PCNA is a nucleotide exchange factor for the clamp loader ATPase complex.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 122, Issue 46, Page e2518834122, Year 2025
Publish date	Nov 18, 2025
Authors	Joshua Pajak / Jacob T Landeck / Xingchen Liu / Krishna Anand / Sasha Litvak / Brian A Kelch /
PubMed Abstract	All life requires loading ring-shaped sliding clamp protein complexes onto DNA. The sliding clamp loader is a conserved AAA+ ATPase that binds the sliding clamp, opens the ring, and places it onto ...All life requires loading ring-shaped sliding clamp protein complexes onto DNA. The sliding clamp loader is a conserved AAA+ ATPase that binds the sliding clamp, opens the ring, and places it onto DNA. While recent structural work on both the canonical and "alternative" clamp loaders has shed light into how these machines perform their task once, it remains unclear how clamp loaders are recycled to load multiple sliding clamps. Here, we present structures of the clamp loader Replication Factor C (RFC) in absence of sliding clamp or supplemented nucleotide. Our structures indicate that RFC holds onto ADP tightly in at least two of its four ATPase active sites, suggesting that nucleotide exchange is regulated. Our molecular dynamics simulations and biochemical data indicate that binding of the sliding clamp Proliferating Cell Nuclear Antigen (PCNA) causes rapid exchange of tightly bound ADP. Our data suggest that PCNA acts as a nucleotide exchange factor (NEF) by prying apart adjacent subunits, providing a pathway for ADP release. We propose that, by using its own substrate as a NEF, RFC excludes off-pathway states that would arise from binding DNA prior to PCNA.
External links	Proc Natl Acad Sci U S A / PubMed:41231947 / PubMed Central
Methods	EM (single particle)
Resolution	2.57 - 2.63 Å
Structure data	71572 9peo EMDB-71572, PDB-9peo: Structure of the S. cerevisiae clamp loader Replication Factor C (RFC) with mixed nucleotide occupancy Method: EM (single particle) / Resolution: 2.57 Å 71574 9per EMDB-71574, PDB-9per: Structure of the S. cerevisiae clamp loader Replication Factor C (RFC) with mixed nucleotide occupancy Method: EM (single particle) / Resolution: 2.57 Å 71575 9pes EMDB-71575, PDB-9pes: Structure of the S. cerevisiae clamp loader Replication Factor C (RFC) with mixed nucleotide occupancy Method: EM (single particle) / Resolution: 2.59 Å 71576 9pet EMDB-71576, PDB-9pet: Structure of the S. cerevisiae clamp loader Replication Factor C (RFC) with mixed nucleotide occupancy Method: EM (single particle) / Resolution: 2.57 Å 71577 9peu EMDB-71577, PDB-9peu: Structure of the S. cerevisiae clamp loader Replication Factor C (RFC) with mixed nucleotide occupancy Method: EM (single particle) / Resolution: 2.62 Å 71578 9pev EMDB-71578, PDB-9pev: Structure of the S. cerevisiae clamp loader Replication Factor C (RFC) with mixed nucleotide occupancy Method: EM (single particle) / Resolution: 2.63 Å
Chemicals	ChemComp-ACT: ACETATE ION ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying moleculeYM
Source	saccharomyces cerevisiae (brewer's yeast)
Keywords	REPLICATION / AAA+ ATPase / Rossmann Fold / Complex / DNA replication