5L2D

Streptococcal surface adhesin - CshA NR2

5L2D の概要

• エントリーDOI: 10.2210/pdb5l2d/pdb
• 分子名称: Surface-associated protein CshA (2 entities in total)
• 機能のキーワード: streptococcus, adhesin, cell adhesion
• 由来する生物種: Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288)
• 細胞内の位置: Secreted : A8AWJ3
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 147104.05

構造登録者

Back, C.R.,Race, P.R.,Jenkinson, H.F. (登録日: 2016-08-01, 公開日: 2016-12-14, 最終更新日: 2024-05-08)

主引用文献

Back, C.R.,Sztukowska, M.N.,Till, M.,Lamont, R.J.,Jenkinson, H.F.,Nobbs, A.H.,Race, P.R.
The Streptococcus gordonii Adhesin CshA Protein Binds Host Fibronectin via a Catch-Clamp Mechanism.
J. Biol. Chem., 292:1538-1549, 2017

PubMed Abstract: Adherence of bacteria to biotic or abiotic surfaces is a prerequisite for host colonization and represents an important step in microbial pathogenicity. This attachment is facilitated by bacterial adhesins at the cell surface. Because of their size and often elaborate multidomain architectures, these polypeptides represent challenging targets for detailed structural and functional characterization. The multifunctional fibrillar adhesin CshA, which mediates binding to both host molecules and other microorganisms, is an important determinant of colonization by Streptococcus gordonii, an oral commensal and opportunistic pathogen of animals and humans. CshA binds the high-molecular-weight glycoprotein fibronectin (Fn) via an N-terminal non-repetitive region, and this protein-protein interaction has been proposed to promote S. gordonii colonization at multiple sites within the host. However, the molecular details of how these two proteins interact have yet to be established. Here we present a structural description of the Fn binding N-terminal region of CshA, derived from a combination of X-ray crystallography, small angle X-ray scattering, and complementary biophysical methods. In vitro binding studies support a previously unreported two-state "catch-clamp" mechanism of Fn binding by CshA, in which the disordered N-terminal domain of CshA acts to "catch" Fn, via formation of a rapidly assembled but also readily dissociable pre-complex, enabling its neighboring ligand binding domain to tightly clamp the two polypeptides together. This study presents a new paradigm for target binding by a bacterial adhesin, the identification of which will inform future efforts toward the development of anti-adhesive agents that target S. gordonii and related streptococci.

PubMed: 27920201
DOI: 10.1074/jbc.M116.760975

実験手法

X-RAY DIFFRACTION (2.66 Å)