3AIZ
Crystal structure of PCNA2-PCNA3 complex from Sulfolobus tokodaii (P21212)
Summary for 3AIZ
Entry DOI | 10.2210/pdb3aiz/pdb |
Related | 3AIX |
Descriptor | DNA polymerase sliding clamp B, DNA polymerase sliding clamp C, SULFATE ION, ... (4 entities in total) |
Functional Keywords | protein-protein complex, replication |
Biological source | Sulfolobus tokodaii More |
Total number of polymer chains | 4 |
Total formula weight | 110644.85 |
Authors | Kawai, A.,Higuchi, S.,Miyamoto, S. (deposition date: 2010-05-18, release date: 2011-05-18, Last modification date: 2023-11-01) |
Primary citation | Kawai, A.,Hashimoto, H.,Higuchi, S.,Tsunoda, M.,Sato, M.,Nakamura, K.T.,Miyamoto, S. A novel heterotetrameric structure of the crenarchaeal PCNA2-PCNA3 complex J.Struct.Biol., 174:443-450, 2011 Cited by PubMed Abstract: Proliferating cell nuclear antigen (PCNA) is a key protein that orchestrates the arrangement of DNA-processing proteins on DNA during DNA metabolism. In crenarchaea, PCNA forms a heterotrimer (PCNA123) consisting of PCNA1, PCNA2, and PCNA3, while in most eukaryotes and many archaea PCNAs form a homotrimer. Interestingly, unique oligomeric PCNAs from Sulfolobus tokodaii were reported in which PCNA2 and PCNA3 form a heterotrimer without PCNA1. In this paper, we describe the crystal structure of the stoPCNA2-stoPCNA3 complex. While most DNA sliding clamps form ring-shaped structures, our crystal structure showed an elliptic ring-like heterotetrameric complex, differing from a previous reports. Furthermore, we investigated the composition and the dimension of the stoPCNA2-stoPCNA3 complex in the solution using gel-filtration column chromatography and small-angle X-ray scattering analyses, respectively. These results indicate that stoPCNA2 and stoPCNA3 form the heterotetramer in solution. Based on our heterotetrameric structure, we propose a possible biological role for the heterotetrameric complex as a Holliday junction clamp. PubMed: 21352919DOI: 10.1016/j.jsb.2011.02.006 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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