5okc

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Crystal structure of the Ctf18-1-8 module from Ctf18-RFCCrystal structure of the Ctf18-1-8 module from Ctf18-RFC

Structural highlights

5okc is a 6 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DCC1_YEAST Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA.[1] [2]

Publication Abstract from PubMed

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 varepsilon. 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 varepsilon throughout normal replication as the leading strand clamp loader. We also show that Pol varepsilon and double-stranded DNA compete to bind the same winged-helix domain on Dcc1, with Pol varepsilon being the preferred binding partner, thus suggesting that there are two alternative pathways to recruit Ctf18-RFC to sites of replication.

Structural Basis for the Recruitment of Ctf18-RFC to the Replisome.,Grabarczyk DB, Silkenat S, Kisker C Structure. 2017 Dec 6. pii: S0969-2126(17)30357-X. doi:, 10.1016/j.str.2017.11.004. PMID:29225079[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Mayer ML, Gygi SP, Aebersold R, Hieter P. Identification of RFC(Ctf18p, Ctf8p, Dcc1p): an alternative RFC complex required for sister chromatid cohesion in S. cerevisiae. Mol Cell. 2001 May;7(5):959-70. PMID:11389843
  2. Bylund GO, Burgers PM. Replication protein A-directed unloading of PCNA by the Ctf18 cohesion establishment complex. Mol Cell Biol. 2005 Jul;25(13):5445-55. PMID:15964801 doi:http://dx.doi.org/25/13/5445
  3. Grabarczyk DB, Silkenat S, Kisker C. Structural Basis for the Recruitment of Ctf18-RFC to the Replisome. Structure. 2017 Dec 6. pii: S0969-2126(17)30357-X. doi:, 10.1016/j.str.2017.11.004. PMID:29225079 doi:http://dx.doi.org/10.1016/j.str.2017.11.004

5okc, resolution 2.30Å

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