6FVM

Mutant DNA polymerase sliding clamp from Escherichia coli with bound P7 peptide

6FVM の概要

• エントリーDOI: 10.2210/pdb6fvm/pdb
• 分子名称: Beta sliding clamp, P7 peptide, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: dna sliding clamp, dna binding protein
• 由来する生物種: Escherichia coli O157:H7; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 85409.85

構造登録者

Martiel, I.,Andre, C.,Olieric, V.,Guichard, G.,Burnouf, D. (登録日: 2018-03-04, 公開日: 2019-04-10, 最終更新日: 2024-10-23)

主引用文献

Andre, C.,Martiel, I.,Wolff, P.,Landolfo, M.,Lorber, B.,Silva da Veiga, C.,Dejaegere, A.,Dumas, P.,Guichard, G.,Olieric, V.,Wagner, J.G.,Burnouf, D.Y.
Peptide Interactions on Bacterial Sliding Clamps.
Acs Infect Dis., 2019

PubMed Abstract: Bacterial sliding clamps control the access of DNA polymerases to the replication fork and are appealing targets for antibacterial drug development. It is therefore essential to decipher the polymerase-clamp binding mode across various bacterial species. Here, two residues of the E. coli clamp binding pocket, S and M, and their cognate residues in M. tuberculosis and B. subtilis clamps, were mutated. The effects of these mutations on the interaction of a model peptide with these variant clamps were evaluated by thermodynamic, molecular dynamics, X-rays crystallography, and biochemical analyses. M and corresponding residues in Gram positive clamps occupy a strategic position where a mobile residue is essential for an efficient peptide interaction. S has a more subtle function that modulates the pocket folding dynamics, while the equivalent residue in B. subtilis is essential for polymerase activity and might therefore be a Gram positive-specific molecular marker. Finally, the peptide binds through an induced-fit process to Gram negative and positive pockets, but the complex stability varies according to a pocket-specific network of interactions.

PubMed: 30912430
DOI: 10.1021/acsinfecdis.9b00089

実験手法

X-RAY DIFFRACTION (1.631 Å)