1OK7

A Conserved protein binding-site on Bacterial Sliding Clamps

1OK7 の概要

• エントリーDOI: 10.2210/pdb1ok7/pdb
• 関連するPDBエントリー: 1JQJ 1JQL 2POL
• 分子名称: DNA POLYMERASE III, DNA POLYMERASE IV (3 entities in total)
• 機能のキーワード: transferase, dna polymerase iv, peptide inhibition, sliding clamp, translesion synthesis, transferase; dna-directed dna polymerase, dna replication
• 由来する生物種: ESCHERICHIA COLI; 詳細
• 細胞内の位置: Cytoplasm : Q47155
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 83087.20

構造登録者

Burnouf, D.Y.,Olieric, V.,Wagner, J.,Fujii, S.,Reinbolt, J.,Fuchs, R.P.P.,Dumas, P. (登録日: 2003-07-18, 公開日: 2004-07-15, 最終更新日: 2023-12-13)

主引用文献

Burnouf, D.Y.,Olieric, V.,Wagner, J.,Fujii, S.,Reinbolt, J.,Fuchs, R.P.P.,Dumas, P.
Structural and Biochemical Analysis of Sliding Clamp/Ligand Interactions Suggest a Competition between Replicative and Translesion DNA Polymerases
J.Mol.Biol., 335:1187-, 2004

PubMed Abstract: Most DNA polymerases interact with their cognate processive replication factor through a small peptide, this interaction being absolutely required for their function in vivo. We have solved the crystal structure of a complex between the beta sliding clamp of Escherichia coli and the 16 residue C-terminal peptide of Pol IV (P16). The seven C-terminal residues bind to a pocket located at the surface of one beta monomer. This region was previously identified as the binding site of another beta clamp binding protein, the delta subunit of the gamma complex. We show that peptide P16 competitively prevents beta-clamp-mediated stimulation of both Pol IV and alpha subunit DNA polymerase activities, suggesting that the site of interaction of the alpha subunit with beta is identical with, or overlaps that of Pol IV. This common binding site for delta, Pol IV and alpha subunit is shown to be formed by residues that are highly conserved among many bacterial beta homologs, thus defining an evolutionarily conserved hydrophobic crevice for sliding clamp ligands and a new target for antibiotic drug design.

PubMed: 14729336
DOI: 10.1016/J.JMB.2003.11.049

実験手法

X-RAY DIFFRACTION (1.65 Å)