1plq

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Revision as of 00:47, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1plq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1plq, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...)
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File:1plq.gif


1plq, resolution 2.3Å

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CRYSTAL STRUCTURE OF THE EUKARYOTIC DNA POLYMERASE PROCESSIVITY FACTOR PCNA

OverviewOverview

The crystal structure of the processivity factor required by eukaryotic, DNA polymerase delta, proliferating cell nuclear antigen (PCNA) from S., cerevisiae, has been determined at 2.3 A 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 beta 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.

About this StructureAbout this Structure

1PLQ is a Single protein structure of sequence from Saccharomyces cerevisiae with HG as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA., Krishna TS, Kong XP, Gary S, Burgers PM, Kuriyan J, Cell. 1994 Dec 30;79(7):1233-43. PMID:8001157

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