Structural highlights
Publication Abstract from PubMed
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 2A structure of beta-clamp from H. pylori (Hpbeta-clamp), which is one of the critical components of DNA polymerase III. Despite of similarity in the overall fold of eubacterial beta-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 beta-clamp such as alpha subunit of DNA pol III and DNA ligase with identification of beta-clamp binding regions in them and validated by SPR studies. Hpbeta-clamp interacts with DNA ligase in micromolar binding affinity. Moreover, we have successfully determined the co-crystal structure of beta-clamp with peptide from DNA ligase (not reported earlier in prokaryotes) revealing the region from ligase that interacts with beta-clamp.
Structural insight into beta-Clamp and its interaction with DNA Ligase in Helicobacter pylori.,Pandey P, Tarique KF, Mazumder M, Rehman SA, Kumari N, Gourinath S Sci Rep. 2016 Aug 8;6:31181. doi: 10.1038/srep31181. PMID:27499105[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pandey P, Tarique KF, Mazumder M, Rehman SA, Kumari N, Gourinath S. Structural insight into beta-Clamp and its interaction with DNA Ligase in Helicobacter pylori. Sci Rep. 2016 Aug 8;6:31181. doi: 10.1038/srep31181. PMID:27499105 doi:http://dx.doi.org/10.1038/srep31181
