View source for 6rje


==Lysostaphin SH3b P4-G5 complex, homesource dataset==
<StructureSection load='6rje' size='340' side='right'caption='[[6rje]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rje]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_simulans Staphylococcus simulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RJE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K5T:(2~{R})-2-[[(2~{S})-2-[[(4~{R})-5-azanyl-4-[[(2~{S})-2-azanylpropanoyl]amino]-5-oxidanylidene-pentanoyl]amino]-6-[2-[2-[2-[2-(2-azanylethanoylamino)ethanoylamino]ethanoylamino]ethanoylamino]ethanoylamino]hexanoyl]amino]propanoic+acid'>K5T</scene></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=6rje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rje OCA], [https://pdbe.org/6rje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rje RCSB], [https://www.ebi.ac.uk/pdbsum/6rje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rje ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LSTP_STASI LSTP_STASI] Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lysostaphin is a bacteriolytic enzyme targeting peptidoglycan, the essential component of the bacterial cell envelope. It displays a very potent and specific activity toward staphylococci, including methicillin-resistant Staphylococcus aureus. Lysostaphin causes rapid cell lysis and disrupts biofilms, and is therefore a therapeutic agent of choice to eradicate staphylococcal infections. The C-terminal SH3b domain of lysostaphin recognizes peptidoglycans containing a pentaglycine crossbridge and has been proposed to drive the preferential digestion of staphylococcal cell walls. Here we elucidate the molecular mechanism underpinning recognition of staphylococcal peptidoglycan by the lysostaphin SH3b domain. We show that the pentaglycine crossbridge and the peptide stem are recognized by two independent binding sites located on opposite sides of the SH3b domain, thereby inducing a clustering of SH3b domains. We propose that this unusual binding mechanism allows synergistic and structurally dynamic recognition of S. aureus peptidoglycan and underpins the potent bacteriolytic activity of this enzyme.

Two-site recognition of Staphylococcus aureus peptidoglycan by lysostaphin SH3b.,Gonzalez-Delgado LS, Walters-Morgan H, Salamaga B, Robertson AJ, Hounslow AM, Jagielska E, Sabala I, Williamson MP, Lovering AL, Mesnage S Nat Chem Biol. 2019 Nov 4. pii: 10.1038/s41589-019-0393-4. doi:, 10.1038/s41589-019-0393-4. PMID:31686030<ref>PMID:31686030</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6rje" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus simulans]]
[[Category: Lovering AL]]
[[Category: Walters-Morgan H]]