9ISJ

Crystal structure of Klebsiella pneumoniae ZapA

9ISJ の概要

• エントリーDOI: 10.2210/pdb9isj/pdb
• 分子名称: Cell division protein ZapA, CHLORIDE ION (3 entities in total)
• 機能のキーワード: bacterial cell division, cell cycle
• 由来する生物種: Klebsiella pneumoniae (strain 342)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25253.83

構造登録者

Fujita, J.,Hibino, K.,Kagoshima, G.,Kamimura, N.,Kato, Y.,Uehara, R.,Namba, K.,Uchihashi, T.,Matsumura, H. (登録日: 2024-07-18, 公開日: 2025-07-23)

主引用文献

Fujita, J.,Kasai, K.,Hibino, K.,Kagoshima, G.,Kamimura, N.,Tobita, S.,Kato, Y.,Uehara, R.,Namba, K.,Uchihashi, T.,Matsumura, H.
Structural basis for the interaction between the bacterial cell division proteins FtsZ and ZapA.
Nat Commun, 16:5985-5985, 2025

PubMed Abstract: Cell division in most bacteria is regulated by the tubulin homolog FtsZ as well as ZapA, a FtsZ-associated protein. However, how FtsZ and ZapA function coordinately has remained elusive. Here we report the cryo-electron microscopy structure of the ZapA-FtsZ complex at 2.73 Å resolution. The complex forms an asymmetric ladder-like structure, in which the double antiparallel FtsZ protofilament on one side and a single protofilament on the other side are tethered by ZapA tetramers. In the complex, the extensive interactions of FtsZ with ZapA cause a structural change of the FtsZ protofilament, and the formation of the double FtsZ protofilament increases electrostatic repulsion. High-speed atomic force microscopy analysis revealed cooperative interactions of ZapA with FtsZ at a molecular level. Our findings not only provide a structural basis for the interaction between FtsZ and ZapA but also shed light on how ZapA binds to FtsZ protofilaments without disturbing FtsZ dynamics to promote cell division.

PubMed: 40593603
DOI: 10.1038/s41467-025-60940-w

実験手法

X-RAY DIFFRACTION (1.8 Å)