4ES9

Crystal Structure of the adhesin domain of Epf from Streptococcus pyogenes in P21

4ES9 の概要

• エントリーDOI: 10.2210/pdb4es9/pdb
• 関連するPDBエントリー: 4ES8
• 分子名称: Epf (2 entities in total)
• 機能のキーワード: carbohydrate-binding module, fibronectin-like domain, cell adhesion
• 由来する生物種: Streptococcus pyogenes
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 143196.83

構造登録者

Linke, C.,Siemens, N.,Kreikemeyer, B.,Baker, E.N. (登録日: 2012-04-23, 公開日: 2012-09-19, 最終更新日: 2023-09-13)

主引用文献

Linke, C.,Siemens, N.,Oehmcke, S.,Radjainia, M.,Law, R.H.,Whisstock, J.C.,Baker, E.N.,Kreikemeyer, B.
The Extracellular Protein Factor Epf from Streptococcus pyogenes Is a Cell Surface Adhesin That Binds to Cells through an N-terminal Domain Containing a Carbohydrate-binding Module.
J.Biol.Chem., 287:38178-38189, 2012

PubMed Abstract: Streptococcus pyogenes is an exclusively human pathogen. Streptococcal attachment to and entry into epithelial cells is a prerequisite for a successful infection of the human host and requires adhesins. Here, we demonstrate that the multidomain protein Epf from S. pyogenes serotype M49 is a streptococcal adhesin. An epf-deficient mutant showed significantly decreased adhesion to and internalization into human keratinocytes. Cell adhesion is mediated by the N-terminal domain of Epf (EpfN) and increased by the human plasma protein plasminogen. The crystal structure of EpfN, solved at 1.6 Å resolution, shows that it consists of two subdomains: a carbohydrate-binding module and a fibronectin type III domain. Both fold types commonly participate in ligand receptor and protein-protein interactions. EpfN is followed by 18 repeats of a domain classified as DUF1542 (domain of unknown function 1542) and a C-terminal cell wall sorting signal. The DUF1542 repeats are not involved in adhesion, but biophysical studies show they are predominantly α-helical and form a fiber-like stalk of tandem DUF1542 domains. Epf thus conforms with the widespread family of adhesins known as MSCRAMMs (microbial surface components recognizing adhesive matrix molecules), in which a cell wall-attached stalk enables long range interactions via its adhesive N-terminal domain.

PubMed: 22977243
DOI: 10.1074/jbc.M112.376434

実験手法

X-RAY DIFFRACTION (2 Å)