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| | <StructureSection load='3oe3' size='340' side='right'caption='[[3oe3]], [[Resolution|resolution]] 1.51Å' scene=''> | | <StructureSection load='3oe3' size='340' side='right'caption='[[3oe3]], [[Resolution|resolution]] 1.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3oe3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OE3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3oe3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OE3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.51Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3od9|3od9]]</div></td></tr>
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| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STM1249 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oe3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oe3 OCA], [https://pdbe.org/3oe3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oe3 RCSB], [https://www.ebi.ac.uk/pdbsum/3oe3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oe3 ProSAT]</span></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=3oe3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oe3 OCA], [https://pdbe.org/3oe3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oe3 RCSB], [https://www.ebi.ac.uk/pdbsum/3oe3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oe3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8ZPY8_SALTY Q8ZPY8_SALTY] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus typhimurium loeffler 1892]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Buntinx, P]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] |
| - | [[Category: Callewaert, L]] | + | [[Category: Buntinx P]] |
| - | [[Category: Heirbaut, M]] | + | [[Category: Callewaert L]] |
| - | [[Category: Herreweghe, J M.Van]] | + | [[Category: Heirbaut M]] |
| - | [[Category: Leysen, S]] | + | [[Category: Leysen S]] |
| - | [[Category: Michiels, C W]] | + | [[Category: Michiels CW]] |
| - | [[Category: Strelkov, S V]] | + | [[Category: Strelkov SV]] |
| - | [[Category: Beta barrel]] | + | [[Category: Van Herreweghe JM]] |
| - | [[Category: Hydrolase inhibitor]]
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| Structural highlights
Function
Q8ZPY8_SALTY
Publication Abstract from PubMed
Lysozymes play a key role in the innate immune system of vertebrates and invertebrates by hydrolyzing peptidoglycan, a vital component of the bacterial cell wall. Gram-negative bacteria produce various types of lysozyme inhibitors that allow them to survive the bactericidal action of lysozyme when their outer membrane is permeabilized. So far, three lysozyme inhibitor families have been described: the Ivy (inhibitor of vertebrate lysozyme) family, the MliC/PliC (membrane-associated/periplasmic lysozyme inhibitor of C-type lysozyme) family, and the PliI (periplasmic lysozyme inhibitor of I-type lysozyme) family. Here, we report high-resolution crystal structures of Salmonella typhimurium PliC (PliC-St) and Aeromonas hydrophila PliI (PliI-Ah). The structure of PliI-Ah is the first in the recently discovered PliI family of lysozyme inhibitors, while the structure of PliC-St is the first structure of a periplasmic lysozyme inhibitor from the PliC/MliC family. Using small-angle X-ray scattering, we demonstrate that both PliC-St and PliI-Ah form stable dimers in solution. The functional dimer architecture of PliC-St is very different from that of the recently described MliC from Pseudomonas aeruginosa (MliC-Pa), despite the close resemblance of their monomers. Furthermore, PliI-Ah has distinctly different monomer and dimer folds compared to PliC, MliC, and Ivy proteins. Site-directed mutagenesis suggests that the inhibitory action of PliI-Ah proceeds via an insertion of a loop containing the conserved SGxY motif into the active center of I-type lysozymes. This motif is related to the functional SGxxY motif found in the MliC/PliC family.
Molecular Basis of Bacterial Defense against Host Lysozymes: X-ray Structures of Periplasmic Lysozyme Inhibitors PliI and PliC.,Leysen S, Van Herreweghe JM, Callewaert L, Heirbaut M, Buntinx P, Michiels CW, Strelkov SV J Mol Biol. 2011 Feb 4;405(5):1233-45. Epub 2010 Dec 10. PMID:21146533[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leysen S, Van Herreweghe JM, Callewaert L, Heirbaut M, Buntinx P, Michiels CW, Strelkov SV. Molecular Basis of Bacterial Defense against Host Lysozymes: X-ray Structures of Periplasmic Lysozyme Inhibitors PliI and PliC. J Mol Biol. 2011 Feb 4;405(5):1233-45. Epub 2010 Dec 10. PMID:21146533 doi:10.1016/j.jmb.2010.12.007
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