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| | <StructureSection load='4qp5' size='340' side='right'caption='[[4qp5]], [[Resolution|resolution]] 1.26Å' scene=''> | | <StructureSection load='4qp5' size='340' side='right'caption='[[4qp5]], [[Resolution|resolution]] 1.26Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qp5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Stast Stast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QP5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QP5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qp5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_simulans_bv._staphylolyticus Staphylococcus simulans bv. staphylolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QP5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.26Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lxc|4lxc]], [[1qwy|1qwy]], [[2b0p|2b0p]], [[2b13|2b13]], [[2b44|2b44]], [[4bh5|4bh5]], [[3it5|3it5]], [[3it7|3it7]], [[1r77|1r77]], [[4qpb|4qpb]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">U66883.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1287 STAST])</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=4qp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qp5 OCA], [https://pdbe.org/4qp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qp5 RCSB], [https://www.ebi.ac.uk/pdbsum/4qp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qp5 ProSAT]</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=4qp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qp5 OCA], [http://pdbe.org/4qp5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qp5 RCSB], [http://www.ebi.ac.uk/pdbsum/4qp5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qp5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LSTP_STASI LSTP_STASI]] Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysostaphin]] | + | [[Category: Staphylococcus simulans bv. staphylolyticus]] |
| - | [[Category: Stast]]
| + | [[Category: Bardelang PT]] |
| - | [[Category: Bardelang, P T]] | + | [[Category: Bochtler M]] |
| - | [[Category: Bochtler, M]] | + | [[Category: Czapinska H]] |
| - | [[Category: Czapinska, H]] | + | [[Category: Dahms SO]] |
| - | [[Category: Dahms, S O]] | + | [[Category: Jagielska E]] |
| - | [[Category: Jagielska, E]] | + | [[Category: James R]] |
| - | [[Category: James, R]] | + | [[Category: Sabala I]] |
| - | [[Category: Sabala, I]] | + | [[Category: Sharpe JA]] |
| - | [[Category: Sharpe, J A]] | + | [[Category: Than ME]] |
| - | [[Category: Than, M E]] | + | [[Category: Thomas NR]] |
| - | [[Category: Thomas, N R]] | + | |
| - | [[Category: Extracellular]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metallopeptidase]]
| + | |
| - | [[Category: Peptidase family m23]]
| + | |
| - | [[Category: Peptidoglycan]]
| + | |
| - | [[Category: Peptidoglycan amidase]]
| + | |
| Structural highlights
Function
LSTP_STASI Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan.
Publication Abstract from PubMed
Staphylococcus simulans biovar staphylolyticus lysostaphin efficiently cleaves Staphylococcus aureus cell walls. The protein is in late clinical trials as a topical anti-staphylococcal agent, and can be used to prevent staphylococcal growth on artificial surfaces. Moreover, the gene has been both stably engineered into and virally delivered to mice or livestock to obtain resistance against staphylococci. Here, we report the first crystal structure of mature lysostaphin and two structures of its isolated catalytic domain at 3.5, 1.78 and 1.26 A resolution, respectively. The structure of the mature active enzyme confirms its expected organization into catalytic and cell-wall-targeting domains. It also indicates that the domains are mobile with respect to each other because of the presence of a highly flexible peptide linker. The high-resolution structures of the catalytic domain provide details of Zn(2+) coordination and may serve as a starting point for the engineering of lysostaphin variants with improved biotechnological characteristics. STRUCTURED DIGITAL ABSTRACT: lysostaphin by x-ray crystallography (1, 2).
Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans.,Sabala I, Jagielska E, Bardelang PT, Czapinska H, Dahms SO, Sharpe JA, James R, Than ME, Thomas NR, Bochtler M FEBS J. 2014 Sep;281(18):4112-22. doi: 10.1111/febs.12929. Epub 2014 Aug 1. PMID:25039253[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sabala I, Jagielska E, Bardelang PT, Czapinska H, Dahms SO, Sharpe JA, James R, Than ME, Thomas NR, Bochtler M. Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans. FEBS J. 2014 Sep;281(18):4112-22. doi: 10.1111/febs.12929. Epub 2014 Aug 1. PMID:25039253 doi:http://dx.doi.org/10.1111/febs.12929
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