3L48

Crystal structure of the C-terminal domain of the PapC usher

3L48 の概要

• エントリーDOI: 10.2210/pdb3l48/pdb
• 分子名称: Outer membrane usher protein PapC, COBALT (II) ION (3 entities in total)
• 機能のキーワード: ig fold, greek key, cell outer membrane, fimbrium, membrane, transmembrane, transport, transport protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein (By similarity): Q1R2W8
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 51436.29

構造登録者

Ford, B.A.,Hultgren, S.J. (登録日: 2009-12-18, 公開日: 2010-03-02, 最終更新日: 2024-11-06)

主引用文献

Ford, B.,Rego, A.T.,Ragan, T.J.,Pinkner, J.,Dodson, K.,Driscoll, P.C.,Hultgren, S.,Waksman, G.
Structural Homology between the C-Terminal Domain of the PapC Usher and Its Plug.
J.Bacteriol., 192:1824-1831, 2010

PubMed Abstract: P pili are extracellular appendages responsible for the targeting of uropathogenic Escherichia coli to the kidney. They are assembled by the chaperone-usher (CU) pathway of pilus biogenesis involving two proteins, the periplasmic chaperone PapD and the outer membrane assembly platform, PapC. Many aspects of the structural biology of the Pap CU pathway have been elucidated, except for the C-terminal domain of the PapC usher, the structure of which is unknown. In this report, we identify a stable and folded fragment of the C-terminal region of the PapC usher and determine its structure using both X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. These structures reveal a beta-sandwich fold very similar to that of the plug domain, a domain of PapC obstructing its translocation domain. This structural similarity suggests similar functions in usher-mediated pilus biogenesis, playing out at different stages of the process. This structure paves the way for further functional analysis targeting surfaces common to both the plug and the C-terminal domain of PapC.

PubMed: 20118254
DOI: 10.1128/JB.01677-09

実験手法

X-RAY DIFFRACTION (2.1 Å)