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<StructureSection load='6rk4' size='340' side='right'caption='[[6rk4]], [[Resolution|resolution]] 1.43Å' scene=''> | <StructureSection load='6rk4' size='340' side='right'caption='[[6rk4]], [[Resolution|resolution]] 1.43Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6rk4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RK4 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6rk4]] 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=6RK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RK4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.43Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6rk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rk4 OCA], [https://pdbe.org/6rk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rk4 RCSB], [https://www.ebi.ac.uk/pdbsum/6rk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rk4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6rk4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus simulans]] | ||
[[Category: Lovering | [[Category: Lovering AL]] | ||
[[Category: Walters-Morgan | [[Category: Walters-Morgan H]] | ||
Latest revision as of 15:22, 24 January 2024
Lysostaphin SH3b P4-G5 complex, synchrotron datasetLysostaphin SH3b P4-G5 complex, synchrotron dataset
Structural highlights
FunctionLSTP_STASI Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan. Publication Abstract from PubMedLysostaphin 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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