8HHF
The bacterial divisome protein complex FtsB-FtsL-FtsQ
8HHF の概要
| エントリーDOI | 10.2210/pdb8hhf/pdb |
| 関連するPDBエントリー | 8HHG 8HHH |
| 分子名称 | Cell division protein FtsQ, Cell division protein FtsB, Cell division protein FtsL, ... (4 entities in total) |
| 機能のキーワード | bacterial cell division, divisome, ftsb, ftsl, ftsq, ftsblq, ftsqlb, membrane protein complex, heterotrimer, membrane protein |
| 由来する生物種 | Escherichia coli K-12 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 58593.47 |
| 構造登録者 | |
| 主引用文献 | Nguyen, H.T.V.,Chen, X.,Parada, C.,Luo, A.C.,Shih, O.,Jeng, U.S.,Huang, C.Y.,Shih, Y.L.,Ma, C. Structure of the heterotrimeric membrane protein complex FtsB-FtsL-FtsQ of the bacterial divisome. Nat Commun, 14:1903-1903, 2023 Cited by PubMed Abstract: The synthesis of the cell-wall peptidoglycan during bacterial cell division is mediated by a multiprotein machine, called the divisome. The essential membrane protein complex of FtsB, FtsL and FtsQ (FtsBLQ) is at the heart of the divisome assembly cascade in Escherichia coli. This complex regulates the transglycosylation and transpeptidation activities of the FtsW-FtsI complex and PBP1b via coordination with FtsN, the trigger for the onset of constriction. Yet the underlying mechanism of FtsBLQ-mediated regulation is largely unknown. Here, we report the full-length structure of the heterotrimeric FtsBLQ complex, which reveals a V-shaped architecture in a tilted orientation. Such a conformation could be strengthened by the transmembrane and the coiled-coil domains of the FtsBL heterodimer, as well as an extended β-sheet of the C-terminal interaction site involving all three proteins. This trimeric structure may also facilitate interactions with other divisome proteins in an allosteric manner. These results lead us to propose a structure-based model that delineates the mechanism of the regulation of peptidoglycan synthases by the FtsBLQ complex. PubMed: 37019934DOI: 10.1038/s41467-023-37543-4 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.04 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






