7YBD
Crystal structure of sliding DNA clamp of Clostridioides difficile
Summary for 7YBD
| Entry DOI | 10.2210/pdb7ybd/pdb |
| Descriptor | Beta sliding clamp, TRIETHYLENE GLYCOL (3 entities in total) |
| Functional Keywords | dna replication, dna binding protein |
| Biological source | Clostridioides difficile |
| Total number of polymer chains | 1 |
| Total formula weight | 41792.94 |
| Authors | Hishiki, A.,Okazaki, S.,Hara, K.,Hashimoto, H. (deposition date: 2022-06-29, release date: 2022-10-19, Last modification date: 2024-05-29) |
| Primary citation | Hishiki, A.,Okazaki, S.,Hara, K.,Hashimoto, H. Crystal structure of the sliding DNA clamp from the Gram-positive anaerobic bacterium Clostridioides difficile. J.Biochem., 173:13-20, 2022 Cited by PubMed Abstract: The sliding DNA clamp is a ring-shaped protein that encircles DNA within its central channel. It binds to multiple proteins, such as DNA polymerases and DNA repair enzymes, and stimulates their enzymatic activities, thereby playing a crucial role in cell survival and proliferation. Accordingly, the bacterial clamp DnaN is considered to be a promising target for bacterial infection therapy. In this regard, 3D structures of DnaN from pathogenic bacteria are essential for the development of chemical compounds with antimicrobial activity. Here, the crystal structure of DnaN from a Gram-positive bacterium Clostridioides difficile, a human pathogen causing infectious diarrhoea, has been determined at 2.13 Å resolution. A comparison of the structures of DnaN from other bacteria indicates that the structural features of DnaN in terms of overall organization are essentially conserved within Gram-positive and Gram-negative bacteria. However, DnaN from C. difficile has structural differences in the potential binding pocket for partner proteins, implying a non-conventional interaction with its binding partners. Our findings will provide insight into the development of new therapies for C. difficile infection. PubMed: 36166824DOI: 10.1093/jb/mvac079 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.13 Å) |
Structure validation
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