3HI8
Crystal structure of proliferating cell nuclear antigen (PCNA) from Haloferax volcanii
Summary for 3HI8
Entry DOI | 10.2210/pdb3hi8/pdb |
Descriptor | Proliferating cell nuclear antigen PcnA (2 entities in total) |
Functional Keywords | sliding clamp, replication, dna interaction, haloferax volcanii |
Biological source | Haloferax volcanii |
Total number of polymer chains | 6 |
Total formula weight | 160175.96 |
Authors | Morgunova, E.,Gray, F.C.,MacNeill, S.A.,Ladenstein, R. (deposition date: 2009-05-19, release date: 2009-09-29, Last modification date: 2023-09-06) |
Primary citation | Morgunova, E.,Gray, F.C.,Macneill, S.A.,Ladenstein, R. Structural insights into the adaptation of proliferating cell nuclear antigen (PCNA) from Haloferax volcanii to a high-salt environment. Acta Crystallogr.,Sect.D, 65:1081-1088, 2009 Cited by PubMed Abstract: The sliding clamp proliferating cell nuclear antigen (PCNA) plays vital roles in many aspects of DNA replication and repair in eukaryotic cells and in archaea. Realising the full potential of archaea as a model for PCNA function requires a combination of biochemical and genetic approaches. In order to provide a platform for subsequent reverse genetic analysis, PCNA from the halophilic archaeon Haloferax volcanii was subjected to crystallographic analysis. The gene was cloned and expressed in Escherichia coli and the protein was purified by affinity chromatography and crystallized by the vapour-diffusion technique. The structure was determined by molecular replacement and refined at 3.5 A resolution to a final R factor of 23.7% (R(free) = 25%). PCNA from H. volcanii was found to be homotrimeric and to resemble other homotrimeric PCNA clamps but with several differences that appear to be associated with adaptation of the protein to the high intracellular salt concentrations found in H. volcanii cells. PubMed: 19770505DOI: 10.1107/S0907444909029321 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.202 Å) |
Structure validation
Download full validation report