Structure of the heterotrimeric PCNA from Sulfolobus solfataricus

@inproceedings{Williams2006StructureOT,
  title={Structure of the heterotrimeric PCNA from Sulfolobus solfataricus
},
  author={Gareth J. Williams and K A Johnson and Jana Rudolf and Stephen A. McMahon and Lester G. Carter and Muse Oke and Huanting Liu and Garry L. Taylor and Malcolm F White and James H. Naismith},
  booktitle={Acta crystallographica. Section F, Structural biology and crystallization communications},
  year={2006}
}
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… CONTINUE READING