4ES8
Crystal Structure of the adhesin domain of Epf from Streptococcus pyogenes in P212121
Summary for 4ES8
| Entry DOI | 10.2210/pdb4es8/pdb |
| Related | 4ES9 |
| Descriptor | Epf, GLYCEROL, ACETATE ION, ... (6 entities in total) |
| Functional Keywords | carbohydrate-binding module, fibronectin-like domain, adhesin, extracellular, cell adhesion |
| Biological source | Streptococcus pyogenes |
| Total number of polymer chains | 2 |
| Total formula weight | 71870.68 |
| Authors | Linke, C.,Siemens, N.,Kreikemeyer, B.,Baker, E.N. (deposition date: 2012-04-23, release date: 2012-09-19, Last modification date: 2024-02-28) |
| Primary citation | 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 Cited by 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: 22977243DOI: 10.1074/jbc.M112.376434 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.58 Å) |
Structure validation
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