2IX2

Crystal structure of the heterotrimeric PCNA from Sulfolobus solfataricus

Summary for 2IX2

• Entry DOI: 10.2210/pdb2ix2/pdb
• Related: 2IZO
• Descriptor: DNA POLYMERASE SLIDING CLAMP B, DNA POLYMERASE SLIDING CLAMP C, DNA POLYMERASE SLIDING CLAMP A, ... (4 entities in total)
• Functional Keywords: replication, sulfolobus sulfataricus, pcna, dna-binding, dna replication
• Biological source: SULFOLOBUS SOLFATARICUS; More
• Total number of polymer chains: 3
• Total formula weight: 84415.23

Authors

Williams, G.J.,Johnson, K.,McMahon, S.A.,Carter, L.,Oke, M.,Liu, H.,Taylor, G.L.,White, M.F.,Naismith, J.H. (deposition date: 2006-07-05, release date: 2006-10-04, Last modification date: 2023-12-13)

Primary citation

Williams, G.J.,Johnson, K.,Rudolf, J.,Mcmahon, S.A.,Carter, L.,Oke, M.,Liu, H.,Taylor, G.L.,White, M.F.,Naismith, J.H.
Structure of the Heterotrimeric PCNA from Sulfolobus Solfataricus.
Acta Crystallogr.,Sect.F, 62:944-, 2006

PubMed Abstract: PCNA is a ring-shaped protein that encircles DNA, providing a platform for the association of a wide variety of DNA-processing enzymes that utilize the PCNA sliding clamp to maintain proximity to their DNA substrates. PCNA is a homotrimer in eukaryotes, but a heterotrimer in crenarchaea such as Sulfolobus solfataricus. The three proteins are SsoPCNA1 (249 residues), SsoPCNA2 (245 residues) and SsoPCNA3 (259 residues). The heterotrimeric protein crystallizes in space group P2(1), with unit-cell parameters a = 44.8, b = 78.8, c = 125.6 A, beta = 100.5 degrees. The crystal structure of this heterotrimeric PCNA molecule has been solved using molecular replacement. The resulting structure to 2.3 A sheds light on the differential stabilities of the interactions observed between the three subunits and the specificity of individual subunits for partner proteins.

PubMed: 17012780
DOI: 10.1107/S1744309106034075

Experimental method

X-RAY DIFFRACTION (2.2 Å)