4TR6

Crystal structure of DNA polymerase sliding clamp from Bacillus subtilis

4TR6 の概要

• エントリーDOI: 10.2210/pdb4tr6/pdb
• 分子名称: DNA polymerase III subunit beta, SODIUM ION (3 entities in total)
• 機能のキーワード: dna polymerase, sliding clamp, processivity, dna binding protein
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm : P05649
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84769.56

構造登録者

Burnouf, D.,Olieric, V.,Ennifar, E.,Wolff, P. (登録日: 2014-06-14, 公開日: 2014-09-10, 最終更新日: 2024-05-08)

主引用文献

Wolff, P.,Amal, I.,Olieric, V.,Chaloin, O.,Gygli, G.,Ennifar, E.,Lorber, B.,Guichard, G.,Wagner, J.,Dejaegere, A.,Burnouf, D.Y.
Differential Modes of Peptide Binding onto Replicative Sliding Clamps from Various Bacterial Origins.
J.Med.Chem., 57:7565-7576, 2014

PubMed Abstract: Bacterial sliding clamps are molecular hubs that interact with many proteins involved in DNA metabolism through their binding, via a conserved peptidic sequence, into a universally conserved pocket. This interacting pocket is acknowledged as a potential molecular target for the development of new antibiotics. We previously designed short peptides with an improved affinity for the Escherichia coli binding pocket. Here we show that these peptides differentially interact with other bacterial clamps, despite the fact that all pockets are structurally similar. Thermodynamic and modeling analyses of the interactions differentiate between two categories of clamps: group I clamps interact efficiently with our designed peptides and assemble the Escherichia coli and related orthologs clamps, whereas group II clamps poorly interact with the same peptides and include Bacillus subtilis and other Gram-positive clamps. These studies also suggest that the peptide binding process could occur via different mechanisms, which depend on the type of clamp.

PubMed: 25170813
DOI: 10.1021/jm500467a

実験手法

X-RAY DIFFRACTION (1.5 Å)