1clq
CRYSTAL STRUCTURE OF A REPLICATION FORK DNA POLYMERASE EDITING COMPLEX AT 2.7 A RESOLUTION
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| , resolution 2.70Å | |||||||
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| Ligands: | and | ||||||
| Gene: | GENE 43 (Enterobacteria phage RB18) | ||||||
| Activity: | DNA-directed DNA polymerase, with EC number 2.7.7.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
We have solved the crystal structures of the bacteriophage RB69 sliding clamp, its complex with a peptide essential for DNA polymerase interactions, and the DNA polymerase complexed with primer-template DNA. The editing complex structure shows a partially melted duplex DNA exiting from the exonuclease domain at an unexpected angle and significant changes in the protein structure. The clamp complex shows the C-terminal 11 residues of polymerase bound in a hydrophobic pocket, and it allows docking of the editing and clamp structures together. The peptide binds to the sliding clamp at a position identical to that of a replication inhibitor peptide bound to PCNA, suggesting that the replication inhibitor protein p21CIP1 functions by competing with eukaryotic polymerases for the same binding pocket on the clamp.
About this StructureAbout this Structure
1CLQ is a Single protein structure of sequence from Enterobacteria phage rb18. The following page contains interesting information on the relation of 1CLQ with [DNA Polymerase]. Full crystallographic information is available from OCA.
ReferenceReference
Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex., Shamoo Y, Steitz TA, Cell. 1999 Oct 15;99(2):155-66. PMID:10535734
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