|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='4qpb' size='340' side='right'caption='[[4qpb]], [[Resolution|resolution]] 1.78Å' scene=''> | | <StructureSection load='4qpb' size='340' side='right'caption='[[4qpb]], [[Resolution|resolution]] 1.78Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qpb]] is a 2 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=4QPB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QPB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qpb]] is a 2 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=4QPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QPB 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=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]] 1.78Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lxc|4lxc]], [[4qp5|4qp5]], [[1qwy|1qwy]], [[2b0p|2b0p]], [[2b13|2b13]], [[2b44|2b44]], [[1r77|1r77]], [[3it7|3it7]], [[3it5|3it5]], [[4bh5|4bh5]]</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=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lss, U66883.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1286 ATCC 27848])</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=4qpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpb OCA], [https://pdbe.org/4qpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qpb RCSB], [https://www.ebi.ac.uk/pdbsum/4qpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qpb 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=4qpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpb OCA], [http://pdbe.org/4qpb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qpb RCSB], [http://www.ebi.ac.uk/pdbsum/4qpb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qpb 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 == |
| Line 25: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 27848]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysostaphin]] | + | [[Category: Staphylococcus simulans]] |
| - | [[Category: Bardelang, P T]] | + | [[Category: Bardelang PT]] |
| - | [[Category: Bochtler, M]] | + | [[Category: Bochtler M]] |
| - | [[Category: Czapinska, H]] | + | [[Category: Czapinska H]] |
| - | [[Category: Dahms, S O]] | + | [[Category: Dahms SO]] |
| - | [[Category: Jagielska, E]] | + | [[Category: Jagielska E]] |
| - | [[Category: James, R]] | + | [[Category: James R]] |
| - | [[Category: Sabala, I]] | + | [[Category: Sabala I]] |
| - | [[Category: Sharpe, J A]] | + | [[Category: Sharpe JA]] |
| - | [[Category: Than, M E]] | + | [[Category: Than ME]] |
| - | [[Category: Thomas, N R]] | + | [[Category: Thomas NR]] |
| - | [[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
|
