8BH1
Core divisome complex FtsWIQBL from Pseudomonas aeruginosa
8BH1 の概要
| エントリーDOI | 10.2210/pdb8bh1/pdb |
| EMDBエントリー | 16042 |
| 分子名称 | Probable peptidoglycan glycosyltransferase FtsW, Peptidoglycan D,D-transpeptidase FtsI, Cell division protein FtsQ, ... (5 entities in total) |
| 機能のキーワード | bacterial cell division, peptidoglycan synthesis, membrane protein complex, membrane protein |
| 由来する生物種 | Pseudomonas aeruginosa PAO1 詳細 |
| タンパク質・核酸の鎖数 | 5 |
| 化学式量合計 | 166910.69 |
| 構造登録者 | Kaeshammer, L.,van den Ent, F.,Jeffery, M.,Lowe, J. (登録日: 2022-10-28, 公開日: 2023-04-19, 最終更新日: 2025-07-02) |
| 主引用文献 | Kashammer, L.,van den Ent, F.,Jeffery, M.,Jean, N.L.,Hale, V.L.,Lowe, J. Cryo-EM structure of the bacterial divisome core complex and antibiotic target FtsWIQBL. Nat Microbiol, 8:1149-1159, 2023 Cited by PubMed Abstract: In most bacteria, cell division relies on the synthesis of new cell wall material by the multiprotein divisome complex. Thus, at the core of the divisome are the transglycosylase FtsW, which synthesises peptidoglycan strands from its substrate Lipid II, and the transpeptidase FtsI that cross-links these strands to form a mesh, shaping and protecting the bacterial cell. The FtsQ-FtsB-FtsL trimeric complex interacts with the FtsWI complex and is involved in regulating its enzymatic activities; however, the structure of this pentameric complex is unknown. Here, we present the cryogenic electron microscopy structure of the FtsWIQBL complex from Pseudomonas aeruginosa at 3.7 Å resolution. Our work reveals intricate structural details, including an extended coiled coil formed by FtsL and FtsB and the periplasmic interaction site between FtsL and FtsI. Our structure explains the consequences of previously reported mutations and we postulate a possible activation mechanism involving a large conformational change in the periplasmic domain. As FtsWIQBL is central to the divisome, our structure is foundational for the design of future experiments elucidating the precise mechanism of bacterial cell division, an important antibiotic target. PubMed: 37127704DOI: 10.1038/s41564-023-01368-0 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.8 Å) |
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