2ix2 | pdb_00002ix2
Crystal structure of the heterotrimeric PCNA from Sulfolobus solfataricus
Structural highlights
FunctionPCNA1_SACS2 One of the sliding clamp subunits that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. Heterotrimer stimulates the Holliday junction resolvase Hjc. DNA polymerase I, DNA ligase and the flap endonuclease may be constitutively associated with the PCNA heterotrimer forming a scanning complex able to couple DNA synthesis and Okazaki fragment maturation.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPCNA 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. Structure of the heterotrimeric PCNA from Sulfolobus solfataricus.,Williams GJ, Johnson K, Rudolf J, McMahon SA, Carter L, Oke M, Liu H, Taylor GL, White MF, Naismith JH Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):944-8. Epub 2006 Sep 19. PMID:17012780[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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