4RKI

Crystal structure of sliding beta clamp from Helicobacter pylori

4RKI の概要

• エントリーDOI: 10.2210/pdb4rki/pdb
• 分子名称: DNA polymerase III subunit beta (2 entities in total)
• 機能のキーワード: processivity promoting factor, transferase
• 由来する生物種: Helicobacter pylori 26695
• 細胞内の位置: Cytoplasm : O25242
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43309.58

構造登録者

Satyawali, P.,Tarique, K.F.,Abdul Rehman, S.A.,Gourinath, S. (登録日: 2014-10-13, 公開日: 2016-01-13, 最終更新日: 2023-09-20)

主引用文献

Pandey, P.,Tarique, K.F.,Mazumder, M.,Rehman, S.A.,Kumari, N.,Gourinath, S.
Structural insight into beta-Clamp and its interaction with DNA Ligase in Helicobacter pylori.
Sci Rep, 6:31181-31181, 2016

PubMed Abstract: Helicobacter pylori, a gram-negative and microaerophilic bacterium, is the major cause of chronic gastritis, gastric ulcers and gastric cancer. Owing to its central role, DNA replication machinery has emerged as a prime target for the development of antimicrobial drugs. Here, we report 2Å structure of β-clamp from H. pylori (Hpβ-clamp), which is one of the critical components of DNA polymerase III. Despite of similarity in the overall fold of eubacterial β-clamp structures, some distinct features in DNA interacting loops exists that have not been reported previously. The in silico prediction identified the potential binders of β-clamp such as alpha subunit of DNA pol III and DNA ligase with identification of β-clamp binding regions in them and validated by SPR studies. Hpβ-clamp interacts with DNA ligase in micromolar binding affinity. Moreover, we have successfully determined the co-crystal structure of β-clamp with peptide from DNA ligase (not reported earlier in prokaryotes) revealing the region from ligase that interacts with β-clamp.

PubMed: 27499105
DOI: 10.1038/srep31181

実験手法

X-RAY DIFFRACTION (2.05 Å)