1qe4

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

BUILDING A REPLISOME FROM INTERACTING PIECES: SLIDING CLAMP COMPLEXED TO A PEPTIDE FROM DNA POLYMERASE AND A POLYMERASE EDITING COMPLEXBUILDING A REPLISOME FROM INTERACTING PIECES: SLIDING CLAMP COMPLEXED TO A PEPTIDE FROM DNA POLYMERASE AND A POLYMERASE EDITING COMPLEX

Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1qe4 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image