5OKI

Crystal structure of the Ctf18-1-8 module from Ctf18-RFC in complex with a 63 kDa fragment of DNA Polymerase epsilon

Summary for 5OKI

• Entry DOI: 10.2210/pdb5oki/pdb
• Descriptor: DNA polymerase epsilon catalytic subunit A, Sister chromatid cohesion protein DCC1, Chromosome transmission fidelity protein 8, ... (4 entities in total)
• Functional Keywords: clamp loader dna-binding protein dna polymerase winged-helix domain, replication
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Cellular location: Nucleus: P21951 P38877 P49956
• Total number of polymer chains: 8
• Total formula weight: 244488.53

Authors

Grabarczyk, D.B.,Kisker, C. (deposition date: 2017-07-25, release date: 2017-12-20, Last modification date: 2024-11-13)

Primary citation

Grabarczyk, D.B.,Silkenat, S.,Kisker, C.
Structural Basis for the Recruitment of Ctf18-RFC to the Replisome.
Structure, 26:137-144.e3, 2018

PubMed Abstract: Ctf18-RFC is an alternative PCNA loader which plays important but poorly understood roles in multiple DNA replication-associated processes. To fulfill its specialist roles, the Ctf18-RFC clamp loader contains a unique module in which the Dcc1-Ctf8 complex is bound to the C terminus of Ctf18 (the Ctf18-1-8 module). Here, we report the structural and functional characterization of the heterotetrameric complex formed between Ctf18-1-8 and a 63 kDa fragment of DNA polymerase ɛ. Our data reveal that Ctf18-1-8 binds stably to the polymerase and far from its other functional sites, suggesting that Ctf18-RFC could be associated with Pol ɛ throughout normal replication as the leading strand clamp loader. We also show that Pol ɛ and double-stranded DNA compete to bind the same winged-helix domain on Dcc1, with Pol ɛ being the preferred binding partner, thus suggesting that there are two alternative pathways to recruit Ctf18-RFC to sites of replication.

PubMed: 29225079
DOI: 10.1016/j.str.2017.11.004

Experimental method

X-RAY DIFFRACTION (4.5 Å)