5FRQ
Crystal Structure of Helicobacter pylori beta clamp bound to DNA ligase peptide
Summary for 5FRQ
| Entry DOI | 10.2210/pdb5frq/pdb |
| Descriptor | DNA POLYMERASE III SUBUNIT BETA, DNA LIGASE (3 entities in total) |
| Functional Keywords | transferase |
| Biological source | HELICOBACTER PYLORI More |
| Total number of polymer chains | 6 |
| Total formula weight | 176127.79 |
| Authors | Pandey, P.,Gourinath, S. (deposition date: 2015-12-21, release date: 2016-08-17, Last modification date: 2024-01-10) |
| Primary citation | Pandey, P.,Tarique, K.F.,Mazumder, M.,Abdul Rehman, S.A.,Gourinath, S. Structural Insight Into Beta-Clamp and its Interaction with DNA Ligase in Helicobacter Pylori Sci.Rep., 6:31181-, 2016 Cited by 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: 27499105DOI: 10.1038/SREP31181 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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