3L0X

Structure of split yeast PCNA

Summary for 3L0X

• Entry DOI: 10.2210/pdb3l0x/pdb
• Related: 3L0W 3L10
• Descriptor: Proliferating cell nuclear antigen (2 entities in total)
• Functional Keywords: replication, dna damage, dna repair, dna replication, dna-binding, isopeptide bond, nucleus, ubl conjugation
• 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: 29661.74

Authors

Freudenthal, B.D.,Gakhar, L.,Ramaswamy, S.,Washington, M.T. (deposition date: 2009-12-10, release date: 2010-03-23, Last modification date: 2023-09-06)

Primary citation

Freudenthal, B.D.,Gakhar, L.,Ramaswamy, S.,Washington, M.T.
Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange.
Nat.Struct.Mol.Biol., 17:479-484, 2010

PubMed Abstract: DNA synthesis by classical polymerases can be blocked by many lesions. These blocks are overcome by translesion synthesis, whereby the stalled classical, replicative polymerase is replaced by a nonclassical polymerase. In eukaryotes this polymerase exchange requires proliferating cell nuclear antigen (PCNA) monoubiquitination. To better understand the polymerase exchange, we developed a means of producing monoubiquitinated PCNA, by splitting the protein into two self-assembling polypeptides. We determined the X-ray crystal structure of monoubiquitinated PCNA and found that the ubiquitin moieties are located on the back face of PCNA and interact with it through their canonical hydrophobic surface. Moreover, the attachment of ubiquitin does not change PCNA's conformation. We propose that PCNA ubiquitination facilitates nonclassical polymerase recruitment to the back of PCNA by forming a new binding surface for nonclassical polymerases, consistent with a 'tool belt' model of the polymerase exchange.

PubMed: 20305653
DOI: 10.1038/nsmb.1776

Experimental method

X-RAY DIFFRACTION (3 Å)