2IZO

Structure of an Archaeal PCNA1-PCNA2-FEN1 Complex

Summary for 2IZO

• Entry DOI: 10.2210/pdb2izo/pdb
• Related: 2IX2
• Descriptor: FLAP STRUCTURE-SPECIFIC ENDONUCLEASE, DNA POLYMERASE SLIDING CLAMP C, DNA POLYMERASE SLIDING CLAMP B, ... (6 entities in total)
• Functional Keywords: hydrolase, dna repair, dna-binding, endonuclease, metal-binding, excision repair, dna replication, pcna, fen1, nuclease, magnesium
• Biological source: SULFOLOBUS SOLFATARICUS; More
• Total number of polymer chains: 3
• Total formula weight: 94838.13

Authors

Dore, A.S.,Kilkenny, M.L.,Roe, S.M.,Pearl, L.H. (deposition date: 2006-07-25, release date: 2006-09-06, Last modification date: 2023-12-13)

Primary citation

Dore, A.S.,Kilkenny, M.L.,Jones, S.A.,Oliver, A.W.,Roe, S.M.,Bell, S.D.,Pearl, L.H.
Structure of an Archaeal PCNA1-PCNA2-Fen1 Complex: Elucidating PCNA Subunit and Client Enzyme Specificity.
Nucleic Acids Res., 34:4515-, 2006

PubMed Abstract: The archaeal/eukaryotic proliferating cell nuclear antigen (PCNA) toroidal clamp interacts with a host of DNA modifying enzymes, providing a stable anchorage and enhancing their respective processivities. Given the broad range of enzymes with which PCNA has been shown to interact, relatively little is known about the mode of assembly of functionally meaningful combinations of enzymes on the PCNA clamp. We have determined the X-ray crystal structure of the Sulfolobus solfataricus PCNA1-PCNA2 heterodimer, bound to a single copy of the flap endonuclease FEN1 at 2.9 A resolution. We demonstrate the specificity of interaction of the PCNA subunits to form the PCNA1-PCNA2-PCNA3 heterotrimer, as well as providing a rationale for the specific interaction of the C-terminal PIP-box motif of FEN1 for the PCNA1 subunit. The structure explains the specificity of the individual archaeal PCNA subunits for selected repair enzyme 'clients', and provides insights into the co-ordinated assembly of sequential enzymatic steps in PCNA-scaffolded DNA repair cascades.

PubMed: 16945955
DOI: 10.1093/NAR/GKL623

Experimental method

X-RAY DIFFRACTION (2.9 Å)