6rk4: Difference between revisions
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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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RK4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6rk4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27848 Atcc 27848]. 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 [http://oca.weizmann.ac.il/oca-docs/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> | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lss ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1286 ATCC 27848])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysostaphin Lysostaphin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.75 3.4.24.75] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysostaphin Lysostaphin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.75 3.4.24.75] </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=6rk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rk4 OCA], [http://pdbe.org/6rk4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rk4 RCSB], [http://www.ebi.ac.uk/pdbsum/6rk4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rk4 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=6rk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rk4 OCA], [http://pdbe.org/6rk4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rk4 RCSB], [http://www.ebi.ac.uk/pdbsum/6rk4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rk4 ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/LSTP_STASI LSTP_STASI]] Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan. | [[http://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: Atcc 27848]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Lysostaphin]] | [[Category: Lysostaphin]] | ||
Revision as of 20:56, 20 November 2019
Lysostaphin SH3b P4-G5 complex, synchrotron datasetLysostaphin SH3b P4-G5 complex, synchrotron dataset
Structural highlights
Function[LSTP_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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