9BIY

Crystal structure of the periplasmic domain of IgaA from Escherichia coli

9BIY の概要

• エントリーDOI: 10.2210/pdb9biy/pdb
• 分子名称: Intracellular growth attenuator protein igaA, Outer membrane lipoprotein RcsF (3 entities in total)
• 機能のキーワード: periplasmic protein, signal transduction, structural genomics, center for structural biology of infectious diseases, csbid, center for structural genomics of infectious diseases, csgid, signaling protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39231.57

構造登録者

Watanabe, N.,Savchenko, A.,Center for Structural Biology of Infectious Diseases (CSBID),Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2024-04-24, 公開日: 2024-07-17, 最終更新日: 2024-11-13)

主引用文献

Watanabe, N.,Savchenko, A.
Molecular insights into the initiation step of the Rcs signaling pathway.
Structure, 32:1381-, 2024

PubMed Abstract: The Rcs pathway is repressed by the inner membrane protein IgaA under non-stressed conditions. This repression is hypothesized to be relieved by the binding of the outer membrane-anchored RcsF to IgaA. However, the precise mechanism by which RcsF binding triggers the signaling remains unclear. Here, we present the 1.8 Å resolution crystal structure capturing the interaction between IgaA and RcsF. Our comparative structural analysis, examining both the bound and unbound states of the periplasmic domain of IgaA (IgaAp), highlights rotational flexibility within IgaAp. Conversely, the conformation of RcsF remains unchanged upon binding. Our in vivo and in vitro studies do not support the model of a stable complex involving RcsF, IgaAp, and RcsDp. Instead, we demonstrate that the elements beyond IgaAp play a role in the interaction between IgaA and RcsD. These findings collectively allow us to propose a potential mechanism for the signaling across the inner membrane through IgaA.

PubMed: 38964336
DOI: 10.1016/j.str.2024.06.003

実験手法

X-RAY DIFFRACTION (1.8 Å)