TY - JOUR
T1 - Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
AU - Krishna, Talluru S.R.
AU - Kong, Xiang Peng
AU - Gary, Sonja
AU - Burgers, Peter M.
AU - Kuriyan, John
N1 - Funding Information:
We are grateful to Mike O’Donnell for initiating this collaboration, Jacqueline Gulbis and Xiaodong Wu for help with synchrotron data collection, and Craig Ogata and Wayne A. Hendrickson for providing access to and support at beamline X4A. We thank Stephen Burley, Jonathan Goldberg, Zvi Kelman, Joseph P. Kim, lsmail Moarefi, Mike O’Donnell, and Bill Weis for helpful suggestions. This work was supported in part by grants from the National Institutes of Health to P. B. (GM32431) and to J. K. (GM45547). Beamline X4A at the National Synchrotron Lightsource in Brookhaven, New York is supported by the Howard Hughes Medical Institute. Atomic coordinates are being deposited in the Protein Databank and are also available by e-mail ([email protected]).
PY - 1994/12/30
Y1 - 1994/12/30
N2 - The crystal structure of the processivity factor required by eukaryotic DNA polymerase δ, proliferating cell nuclear antigen (PCNA) from S. cerevisiae, has been determined at 2.3 Å resolution. Three PCNA molecules, each containing two topologically identical domains, are tightly associated to form a closed ring. The dimensions and electrostatic properties of the ring suggest that PCNA encircles duplex DNA, providing a DNA-bound platform for the attachment of the polymerase. The trimeric PCNA ring is strikingly similar to the dimeric ring formed by the β subunit (processivity factor) of E. coli DNA polymerase III holoenzyme, with which it shares no significant sequence identity. This structural correspondence further substantiates the mechanistic connection between eukaryotic and prokaryotic DNA replication that has been suggested on biochemical grounds.
AB - The crystal structure of the processivity factor required by eukaryotic DNA polymerase δ, proliferating cell nuclear antigen (PCNA) from S. cerevisiae, has been determined at 2.3 Å resolution. Three PCNA molecules, each containing two topologically identical domains, are tightly associated to form a closed ring. The dimensions and electrostatic properties of the ring suggest that PCNA encircles duplex DNA, providing a DNA-bound platform for the attachment of the polymerase. The trimeric PCNA ring is strikingly similar to the dimeric ring formed by the β subunit (processivity factor) of E. coli DNA polymerase III holoenzyme, with which it shares no significant sequence identity. This structural correspondence further substantiates the mechanistic connection between eukaryotic and prokaryotic DNA replication that has been suggested on biochemical grounds.
UR - http://www.scopus.com/inward/record.url?scp=0028618183&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(94)90014-0
DO - 10.1016/0092-8674(94)90014-0
M3 - Article
C2 - 8001157
AN - SCOPUS:0028618183
SN - 0092-8674
VL - 79
SP - 1233
EP - 1243
JO - Cell
JF - Cell
IS - 7
ER -