3PGE

Structure of sumoylated PCNA

Summary for 3PGE

• Entry DOI: 10.2210/pdb3pge/pdb
• Related: 3L0X
• Descriptor: SUMO-modified proliferating cell nuclear antigen, Proliferating cell nuclear antigen (2 entities in total)
• Functional Keywords: dna replication, dna binding protein
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); More
• Cellular location: Nucleus: P15873 P15873
• Total number of polymer chains: 2
• Total formula weight: 42033.51

Authors

Freudenthal, B.D.,Brogie, J.E.,Gakhar, L.,Washington, T. (deposition date: 2010-11-01, release date: 2010-12-29, Last modification date: 2023-09-06)

Primary citation

Freudenthal, B.D.,Brogie, J.E.,Gakhar, L.,Kondratick, C.M.,Washington, M.T.
Crystal Structure of SUMO-Modified Proliferating Cell Nuclear Antigen.
J.Mol.Biol., 406:9-17, 2011

PubMed Abstract: Eukaryotic proliferating cell nuclear antigen (PCNA) is a replication accessory protein that functions in DNA replication, repair, and recombination. The various functions of PCNA are regulated by posttranslational modifications including mono-ubiquitylation, which promotes translesion synthesis, and sumoylation, which inhibits recombination. To understand how SUMO modification regulates PCNA, we generated a split SUMO-modified PCNA protein and showed that it supports cell viability and stimulates DNA polymerase δ activity. We then determined its X-ray crystal structure and found that SUMO occupies a position on the back face of the PCNA ring, which is distinct from the position occupied by ubiquitin in the structure of ubiquitin-modified PCNA. We propose that the back of PCNA has evolved to be a site of regulation that can be easily modified without disrupting ongoing reactions on the front of PCNA, such as normal DNA replication. Moreover, these modifications likely allow PCNA to function as a tool belt, whereby proteins can be recruited to the replication machinery via the back of PCNA and be held in reserve until needed.

PubMed: 21167178
DOI: 10.1016/j.jmb.2010.12.015

Experimental method

X-RAY DIFFRACTION (2.8 Å)