3GPN
Structure of the non-trimeric form of the E113G PCNA mutant protein
Summary for 3GPN
| Entry DOI | 10.2210/pdb3gpn/pdb |
| Related | 3GPM |
| Descriptor | Proliferating cell nuclear antigen (1 entity in total) |
| Functional Keywords | replication, dna damage, dna repair, dna replication, dna-binding, isopeptide bond, nucleus, ubl conjugation, dna binding protein |
| Biological source | Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast) |
| Cellular location | Nucleus: P15873 |
| Total number of polymer chains | 1 |
| Total formula weight | 28871.99 |
| Authors | Freudenthal, B.D.,Gakhar, L.,Ramaswamy, S.,Washington, M.T. (deposition date: 2009-03-23, release date: 2009-06-16, Last modification date: 2023-09-06) |
| Primary citation | Freudenthal, B.D.,Gakhar, L.,Ramaswamy, S.,Washington, M.T. A charged residue at the subunit interface of PCNA promotes trimer formation by destabilizing alternate subunit interactions. Acta Crystallogr.,Sect.D, 65:560-566, 2009 Cited by PubMed Abstract: Eukaryotic proliferating cell nuclear antigen (PCNA) is an essential replication accessory factor that interacts with a variety of proteins involved in DNA replication and repair. Each monomer of PCNA has an N-terminal domain A and a C-terminal domain B. In the structure of the wild-type PCNA protein, domain A of one monomer interacts with domain B of a neighboring monomer to form a ring-shaped trimer. Glu113 is a conserved residue at the subunit interface in domain A. Two distinct X-ray crystal structures have been determined of a mutant form of PCNA with a substitution at this position (E113G) that has previously been studied because of its effect on translesion synthesis. The first structure was the expected ring-shaped trimer. The second structure was an unanticipated nontrimeric form of the protein. In this nontrimeric form, domain A of one PCNA monomer interacts with domain A of a neighboring monomer, while domain B of this monomer interacts with domain B of a different neighboring monomer. The B-B interface is stabilized by an antiparallel beta-sheet and appears to be structurally similar to the A-B interface observed in the trimeric form of PCNA. The A-A interface, in contrast, is primarily stabilized by hydrophobic interactions. Because the E113G substitution is located on this hydrophobic surface, the A-A interface should be less favorable in the case of the wild-type protein. This suggests that the side chain of Glu113 promotes trimer formation by destabilizing these possible alternate subunit interactions. PubMed: 19465770DOI: 10.1107/S0907444909011329 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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