View source for 5kgz


==Phenol-soluble modulin Beta2==
<StructureSection load='5kgz' size='340' side='right'caption='[[5kgz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5kgz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KGZ FirstGlance]. <br>
</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=5kgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kgz OCA], [https://pdbe.org/5kgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kgz RCSB], [https://www.ebi.ac.uk/pdbsum/5kgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kgz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H9BRQ4_STAAU H9BRQ4_STAAU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Phenol-soluble modulins (PSMs) are peptide virulence factors produced by staphylococci. These peptides contribute to the overall pathogenicity of these bacteria, eliciting multiple immune responses from host cells. Many of the alpha-type PSMs exhibit cytolytic properties and are able to lyse particular eukaryotic cells, including erythrocytes, neutrophils, and leukocytes. In addition, they also appear to contribute to the protection of the bacterial cell from the host immune response through biofilm formation and detachment. In this study, three of these peptide toxins, PSMs alpha1, alpha3, and beta2, normally produced by Staphylococcus aureus, have been synthesized using solid-supported peptide synthesis (SPPS) (PSMalpha1 and PSMalpha3) or made by heterologous expression in Escherichia coli (PSMbeta2). Their three-dimensional structures were elucidated using nuclear magnetic resonance spectroscopy. PSMalpha1 and PSMalpha3 each consist of a single amphipathic helix with a slight bend near the N- and C-termini, respectively. PSMbeta2 contains three amphipathic helices, which fold to produce a "v-like" shape between alpha-helix 2 and alpha-helix 3, with alpha-helix 1 folded over such that it is perpendicular to alpha-helix 3. The availability of three-dimensional structures permits spatial analysis of features and residues proposed to control the biological activity of these peptide toxins.

Solution Structures of Phenol-Soluble Modulins alpha1, alpha3, and beta2, Virulence Factors from Staphylococcus aureus.,Towle KM, Lohans CT, Miskolzie M, Acedo JZ, van Belkum MJ, Vederas JC Biochemistry. 2016 Aug 30;55(34):4798-806. doi: 10.1021/acs.biochem.6b00615. Epub, 2016 Aug 15. PMID:27525453<ref>PMID:27525453</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kgz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Acedo JZ]]
[[Category: Lohans CT]]
[[Category: Miskolzie M]]
[[Category: Towle KM]]
[[Category: Van Belkum MJ]]
[[Category: Vederas JC]]