1CLQ

CRYSTAL STRUCTURE OF A REPLICATION FORK DNA POLYMERASE EDITING COMPLEX AT 2.7 A RESOLUTION

Summary for 1CLQ

• Entry DOI: 10.2210/pdb1clq/pdb
• Descriptor: DNA (5'-D(*GP*CP*GP*GP*AP*AP*CP*TP*AP*CP*T)-3'), DNA (5'-D(*AP*GP*TP*AP*GP*TP*TP*CP*CP*GP*CP*G)-3'), PROTEIN (DNA POLYMERASE), ... (6 entities in total)
• Functional Keywords: dna polymerase, gp43, proofreading, editing, replication, transferase-dna complex, transferase/dna
• Biological source: Enterobacteria phage RB69; More
• Total number of polymer chains: 3
• Total formula weight: 112583.67

Authors

Shamoo, Y.,Steitz, T.A. (deposition date: 1999-04-30, release date: 1999-10-28, Last modification date: 2023-08-02)

Primary citation

Shamoo, Y.,Steitz, T.A.
Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex.
Cell(Cambridge,Mass.), 99:155-166, 1999

PubMed Abstract: 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.

PubMed: 10535734
DOI: 10.1016/S0092-8674(00)81647-5

Experimental method

X-RAY DIFFRACTION (2.7 Å)