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==Crystal Structure of the adhesin domain of Epf from Streptococcus pyogenes in P212121==
==Crystal Structure of the adhesin domain of Epf from Streptococcus pyogenes in P212121==
<StructureSection load='4es8' size='340' side='right' caption='[[4es8]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
<StructureSection load='4es8' size='340' side='right'caption='[[4es8]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4es8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes_m49_591 Streptococcus pyogenes m49 591]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ES8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ES8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4es8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_M49_591 Streptococcus pyogenes M49 591]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ES8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ES8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4es9|4es9]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SpyoM01000212 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294934 Streptococcus pyogenes M49 591])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4es8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4es8 OCA], [https://pdbe.org/4es8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4es8 RCSB], [https://www.ebi.ac.uk/pdbsum/4es8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4es8 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4es8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4es8 OCA], [http://pdbe.org/4es8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4es8 RCSB], [http://www.ebi.ac.uk/pdbsum/4es8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4es8 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A0A0H3BY62_STRPZ A0A0H3BY62_STRPZ]
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 internalisation 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 A 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 Domain of Unknown Function 1542 (DUF1542) and a C-terminal cell wall sorting signal. The DUF1542 repeats are not involved in adhesion, but biophysical studies show they are predominantly alpha-helical and form a fibre-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.
 
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.,Linke C, Siemens N, Oehmcke S, Radjainia M, Law RH, Whisstock JC, Baker EN, Kreikemeyer B J Biol Chem. 2012 Sep 12. PMID:22977243<ref>PMID:22977243</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4es8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Streptococcus pyogenes m49 591]]
[[Category: Large Structures]]
[[Category: Baker, E N]]
[[Category: Streptococcus pyogenes M49 591]]
[[Category: Kreikemeyer, B]]
[[Category: Baker EN]]
[[Category: Linke, C]]
[[Category: Kreikemeyer B]]
[[Category: Siemens, N]]
[[Category: Linke C]]
[[Category: Adhesin]]
[[Category: Siemens N]]
[[Category: Carbohydrate-binding module]]
[[Category: Cell adhesion]]
[[Category: Extracellular]]
[[Category: Fibronectin-like domain]]
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