3LIU

Crystal structure of Putative cell adhesion protein (YP_001304840.1) from Parabacteroides distasonis ATCC 8503 at 2.05 A resolution

3LIU の概要

• エントリーDOI: 10.2210/pdb3liu/pdb
• 分子名称: Putative cell adhesion protein, CHLORIDE ION, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, cell adhesion
• 由来する生物種: Parabacteroides distasonis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88103.64

構造登録者

Joint Center for Structural Genomics (JCSG) (登録日: 2010-01-25, 公開日: 2010-02-09, 最終更新日: 2024-11-06)

主引用文献

Xu, Q.,Shoji, M.,Shibata, S.,Naito, M.,Sato, K.,Elsliger, M.A.,Grant, J.C.,Axelrod, H.L.,Chiu, H.J.,Farr, C.L.,Jaroszewski, L.,Knuth, M.W.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Curtis, M.A.,Nakayama, K.,Wilson, I.A.
A Distinct Type of Pilus from the Human Microbiome.
Cell, 165:690-703, 2016

PubMed Abstract: Pili are proteinaceous polymers of linked pilins that protrude from the cell surface of many bacteria and often mediate adherence and virulence. We investigated a set of 20 Bacteroidia pilins from the human microbiome whose structures and mechanism of assembly were unknown. Crystal structures and biochemical data revealed a diverse protein superfamily with a common Greek-key β sandwich fold with two transthyretin-like repeats that polymerize into a pilus through a strand-exchange mechanism. The assembly mechanism of the central, structural pilins involves proteinase-assisted removal of their N-terminal β strand, creating an extended hydrophobic groove that binds the C-terminal donor strands of the incoming pilin. Accessory pilins at the tip and base have unique structural features specific to their location, allowing initiation or termination of the assembly. The Bacteroidia pilus, therefore, has a biogenesis mechanism that is distinct from other known pili and likely represents a different type of bacterial pilus.

PubMed: 27062925
DOI: 10.1016/j.cell.2016.03.016

実験手法

X-RAY DIFFRACTION (2.05 Å)