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| | ==Crystal structure of Staphylococcal Superantigen-Like protein 11 in complex with Sialyl Lewis X== | | ==Crystal structure of Staphylococcal Superantigen-Like protein 11 in complex with Sialyl Lewis X== |
| - | <StructureSection load='2rdg' size='340' side='right' caption='[[2rdg]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='2rdg' size='340' side='right'caption='[[2rdg]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rdg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RDG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RDG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rdg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RDG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</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]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rdh|2rdh]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=PRD_900122:Sialyl-Lewis+X+antigen,+alpha+anomer'>PRD_900122</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSL11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=2rdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rdg OCA], [https://pdbe.org/2rdg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rdg RCSB], [https://www.ebi.ac.uk/pdbsum/2rdg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rdg 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=2rdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rdg OCA], [http://pdbe.org/2rdg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rdg RCSB], [http://www.ebi.ac.uk/pdbsum/2rdg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rdg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SLL11_STAAU SLL11_STAAU] Secreted protein that plays a role in the inhibition of host immune system. Targets myeloid cells such as monocytes or granulocytes through binding with sialyllactosamine-containing glycoproteins (PubMed:18045383). Prevents initial rolling of neutrophils toward the site of infection by interacting with host SELPLG (PubMed:18045383). Disrupts neutrophil motility by induction of cell adhesion via interacting with glycans but independently of SELPLG (PubMed:30862940).<ref>PMID:18045383</ref> <ref>PMID:30862940</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker, E N]] | + | [[Category: Large Structures]] |
| - | [[Category: Baker, H]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Chung, M C]] | + | [[Category: Baker EN]] |
| - | [[Category: Fraser, J D]] | + | [[Category: Baker H]] |
| - | [[Category: Langley, R J]] | + | [[Category: Chung MC]] |
| - | [[Category: Wines, B D]] | + | [[Category: Fraser JD]] |
| - | [[Category: Beta grasp]] | + | [[Category: Langley RJ]] |
| - | [[Category: Ob fold]] | + | [[Category: Wines BD]] |
| - | [[Category: Protein-carbohydrate complex]]
| + | |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
2rdg is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.6Å |
| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
SLL11_STAAU Secreted protein that plays a role in the inhibition of host immune system. Targets myeloid cells such as monocytes or granulocytes through binding with sialyllactosamine-containing glycoproteins (PubMed:18045383). Prevents initial rolling of neutrophils toward the site of infection by interacting with host SELPLG (PubMed:18045383). Disrupts neutrophil motility by induction of cell adhesion via interacting with glycans but independently of SELPLG (PubMed:30862940).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Staphylococcus aureus is a major pathogen that produces a family of 14 staphylococcal superantigen-like (SSL) proteins, which are structurally similar to superantigens but do not stimulate T cells. SSL11 is one member of the family that is found in all staphylococcal strains. Recombinant SSL11 bound to granulocytes and monocytes through a sialic acid-dependent mechanism and was rapidly internalized. SSL11 also bound to sialic acid-containing glycoproteins, such as the Fc receptor for IgA (FcalphaRI) and P-selectin glycoprotein ligand-1 (PSGL-1), and inhibited neutrophil attachment to a P-selectin-coated surface. Biosensor analysis of two SSL11 alleles binding to sialyl Lewis X [sLe(x)- Neu5Acalpha2-3Galbeta1-4(Fuc1-3)GlcNAc] coupled to bovine serum albumin gave dissociation constants of 0.7 and 7 mum respectively. Binding of SSL11 to a glycan array revealed specificity for glycans containing the trisaccharide sialyllactosamine (sLacNac - Neu5Acalpha2-3Galbeta1-4GlcNAc). A 1.6 A resolution crystal structure of SSL11 complexed with sLe(x) revealed a discrete binding site in the C-terminal beta-grasp domain, with predominant interactions with the sialic acid and galactose residues. A single amino acid mutation in the carbohydrate binding site abolished all SSL11 binding. Thus, SSL11 is a staphylococcal protein that targets myeloid cells by binding sialyllactosamine-containing glycoproteins.
The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition.,Chung MC, Wines BD, Baker H, Langley RJ, Baker EN, Fraser JD Mol Microbiol. 2007 Dec;66(6):1342-55. PMID:18045383[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chung MC, Wines BD, Baker H, Langley RJ, Baker EN, Fraser JD. The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition. Mol Microbiol. 2007 Dec;66(6):1342-55. PMID:18045383 doi:10.1111/j.1365-2958.2007.05989.x
- ↑ Chen C, Yang C, Barbieri JT. Staphylococcal Superantigen-like protein 11 mediates neutrophil adhesion and motility arrest, a unique bacterial toxin action. Sci Rep. 2019 Mar 12;9(1):4211. PMID:30862940 doi:10.1038/s41598-019-40817-x
- ↑ Chung MC, Wines BD, Baker H, Langley RJ, Baker EN, Fraser JD. The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition. Mol Microbiol. 2007 Dec;66(6):1342-55. PMID:18045383 doi:10.1111/j.1365-2958.2007.05989.x
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