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3AIX

Crystal structure of PCNA2-PCNA3 complex from Sulfolobus tokodaii (I222)

Summary for 3AIX
Entry DOI10.2210/pdb3aix/pdb
Related3AIZ
DescriptorDNA polymerase sliding clamp C, DNA polymerase sliding clamp B, SULFATE ION, ... (4 entities in total)
Functional Keywordsprotein-protein complex, replication
Biological sourceSulfolobus tokodaii
More
Total number of polymer chains2
Total formula weight55322.42
Authors
Kawai, A.,Higuchi, S.,Miyamoto, S. (deposition date: 2010-05-18, release date: 2011-05-18, Last modification date: 2023-11-01)
Primary citationKawai, 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: 21352919
DOI: 10.1016/j.jsb.2011.02.006
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

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数据于2024-11-13公开中

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