7YBD
Crystal structure of sliding DNA clamp of Clostridioides difficile
7YBD の概要
エントリーDOI | 10.2210/pdb7ybd/pdb |
分子名称 | Beta sliding clamp, TRIETHYLENE GLYCOL (3 entities in total) |
機能のキーワード | dna replication, dna binding protein |
由来する生物種 | Clostridioides difficile |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 41792.94 |
構造登録者 | Hishiki, A.,Okazaki, S.,Hara, K.,Hashimoto, H. (登録日: 2022-06-29, 公開日: 2022-10-19, 最終更新日: 2024-05-29) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.13 Å) |
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