8A9W

Crystal structure of PulL C-ter domain

8A9W の概要

• エントリーDOI: 10.2210/pdb8a9w/pdb
• 分子名称: Type II secretion system protein L, SULFATE ION (3 entities in total)
• 機能のキーワード: type ii secretion system, assembly platform, klebsiella oxytoca, ferredoxin-like domain, structural protein
• 由来する生物種: Klebsiella oxytoca
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8881.00

構造登録者

Dazzoni, R.,Li, Y.,Lopez-Castilla, A.,Brier, S.,Mechaly, A.,Cordier, F.,Haouz, A.,Nilges, M.,Francetic, O.,Bardiaux, B.,Izadi-Pruneyre, N. (登録日: 2022-06-29, 公開日: 2023-01-11, 最終更新日: 2024-05-01)

主引用文献

Dazzoni, R.,Li, Y.,Lopez-Castilla, A.,Brier, S.,Mechaly, A.,Cordier, F.,Haouz, A.,Nilges, M.,Francetic, O.,Bardiaux, B.,Izadi-Pruneyre, N.
Structure and dynamic association of an assembly platform subcomplex of the bacterial type II secretion system.
Structure, 31:152-, 2023

PubMed Abstract: Type II secretion systems (T2SSs) allow diderm bacteria to secrete hydrolytic enzymes, adhesins, or toxins important for growth and virulence. To promote secretion of folded proteins, T2SSs assemble periplasmic filaments called pseudopili or endopili at an inner membrane subcomplex, the assembly platform (AP). Here, we combined biophysical approaches, nuclear magnetic resonance (NMR) and X-ray crystallography, to study the Klebsiella AP components PulL and PulM. We determined the structure and associations of their periplasmic domains and describe the structure of the heterodimer formed by their ferredoxin-like domains. We show how structural complementarity and plasticity favor their association during the secretion process. Cysteine scanning and crosslinking data provided additional constraints to build a structural model of the PulL-PulM assembly in the cellular context. Our structural and functional insights, together with the relative cellular abundance of its components, support the role of AP as a dynamic hub that orchestrates pilus polymerization.

PubMed: 36586404
DOI: 10.1016/j.str.2022.12.003

実験手法

X-RAY DIFFRACTION (1.895 Å)