3FIP

Crystal structure of Usher PapC translocation pore

3FIP の概要

• エントリーDOI: 10.2210/pdb3fip/pdb
• 関連するPDBエントリー: 2VQI
• 分子名称: Outer membrane usher protein papC (1 entity in total)
• 機能のキーワード: beta barrel, protein translocase, cell membrane, 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: P07110
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 109722.27

構造登録者

Huang, Y.,Deisenhofer, J. (登録日: 2008-12-12, 公開日: 2009-09-08, 最終更新日: 2024-02-21)

主引用文献

Huang, Y.,Smith, B.S.,Chen, L.X.,Baxter, R.H.,Deisenhofer, J.
Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC.
Proc.Natl.Acad.Sci.USA, 106:7403-7407, 2009

PubMed Abstract: Ushers constitute a family of bacterial outer membrane proteins responsible for the assembly and secretion of surface organelles such as the pilus. The structure at 3.15-A resolution of the usher pyelonephritis-associated pili C (PapC) translocation domain reveals a 24-stranded kidney-shaped beta-barrel, occluded by an internal plug domain. The dimension of the pore allows tandem passage of individual folded pilus subunits in an upright pilus growth orientation, but is insufficient for accommodating donor strand exchange. The molecular packing revealed by the crystal structure shows that 2 PapC molecules in head-to-head orientation interact via exposed beta-strand edges, which could be the preferred dimer interaction in solution. In vitro reconstitution of fiber assemblies suggest that PapC monomers may be sufficient for fiber assembly and secretion; both the plug domain and the C-terminal domain of PapC are required for filament assembly, whereas the N-terminal domain is mainly responsible for recruiting the chaperone-subunit complexes to the usher. The plug domain has a dual function: gating the beta-pore and participating in pilus assembly.

PubMed: 19380723
DOI: 10.1073/pnas.0902789106

実験手法

X-RAY DIFFRACTION (3.154 Å)