Structural highlights
Function
CLAMP_BPR69 Sliding clamp that encircles the genomic DNA and links the DNA polymerase to the template to control the processivity of DNA synthesis. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. Interaction with the sliding-clamp-loader opens the sliding clamp so that it can be loaded around the DNA template. During transcription, encircles the DNA and tethers host RNA polymerase (RNAP) to it.[HAMAP-Rule:MF_04161]
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 PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shamoo Y, Steitz TA. Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex. Cell. 1999 Oct 15;99(2):155-66. PMID:10535734
