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| <StructureSection load='6rhv' size='340' side='right'caption='[[6rhv]], [[Resolution|resolution]] 2.29Å' scene=''> | | <StructureSection load='6rhv' size='340' side='right'caption='[[6rhv]], [[Resolution|resolution]] 2.29Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6rhv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RHV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RHV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rhv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RHV FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.29Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lukG, ELQ85_15505, EP54_11070, EQ90_09460, HMPREF3211_02235, NCTC10654_02179, NCTC10702_03203, NCTC13131_01350, RK64_10675 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885]), lukH, BTN44_11630, EP54_11065, EQ90_09455, HMPREF3211_02234, NCTC10654_02180, NCTC10702_03204, NCTC13131_01351, NCTC13196_01958, RK64_10680 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885]), Itgam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=6rhv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rhv OCA], [http://pdbe.org/6rhv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rhv RCSB], [http://www.ebi.ac.uk/pdbsum/6rhv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rhv 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=6rhv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rhv OCA], [https://pdbe.org/6rhv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rhv RCSB], [https://www.ebi.ac.uk/pdbsum/6rhv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rhv ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/ITAM_MOUSE ITAM_MOUSE]] Integrin ITGAM/ITGB2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles and pathogens (By similarity). It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin ITGAM/ITGB2 is also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of fibrinogen gamma chain. Regulates neutrophil migration. In association with beta subunit ITGB2/CD18, required for CD177-PRTN3-mediated activation of TNF primed neutrophils (By similarity). May regulate phagocytosis-induced apoptosis in extravasated neutrophils (By similarity). May play a role in mast cell development (By similarity). Required with TYROBP/DAP12 in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (PubMed:18685038).[UniProtKB:P11215]<ref>PMID:18685038</ref> <ref>PMID:8986723</ref> <ref>PMID:9382884</ref> <ref>PMID:9862668</ref> | + | [https://www.uniprot.org/uniprot/LUKL1_STAA8 LUKL1_STAA8] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </div> | | </div> |
| <div class="pdbe-citations 6rhv" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6rhv" style="background-color:#fffaf0;"></div> |
| + | |
| + | ==See Also== |
| + | *[[Cytolysin 3D structures|Cytolysin 3D structures]] |
| + | *[[Integrin 3D structures|Integrin 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
- | [[Category: Badarau, A]] | + | [[Category: Staphylococcus aureus]] |
- | [[Category: Djinovic-Carugo, K]] | + | [[Category: Badarau A]] |
- | [[Category: Milic, D]] | + | [[Category: Djinovic-Carugo K]] |
- | [[Category: Trstenjak, N]] | + | [[Category: Milic D]] |
- | [[Category: Complex]]
| + | [[Category: Trstenjak N]] |
- | [[Category: Leukocidin]]
| + | |
- | [[Category: Octamer]]
| + | |
- | [[Category: Pore-forming toxin]]
| + | |
- | [[Category: Receptor]]
| + | |
- | [[Category: Toxin]]
| + | |
| Structural highlights
Function
LUKL1_STAA8
Publication Abstract from PubMed
Host-pathogen interactions are central to understanding microbial pathogenesis. The staphylococcal pore-forming cytotoxins hijack important immune molecules but little is known about the underlying molecular mechanisms of cytotoxin-receptor interaction and host specificity. Here we report the structures of a staphylococcal pore-forming cytotoxin, leukocidin GH (LukGH), in complex with its receptor (the alpha-I domain of complement receptor 3, CD11b-I), both for the human and murine homologs. We observe 2 binding interfaces, on the LukG and the LukH protomers, and show that human CD11b-I induces LukGH oligomerization in solution. LukGH binds murine CD11b-I weakly and is inactive toward murine neutrophils. Using a LukGH variant engineered to bind mouse CD11b-I, we demonstrate that cytolytic activity does not only require binding but also receptor-dependent oligomerization. Our studies provide an unprecedented insight into bicomponent leukocidin-host receptor interaction, enabling the development of antitoxin approaches and improved animal models to explore these approaches.
Molecular mechanism of leukocidin GH-integrin CD11b/CD18 recognition and species specificity.,Trstenjak N, Milic D, Graewert MA, Rouha H, Svergun D, Djinovic-Carugo K, Nagy E, Badarau A Proc Natl Acad Sci U S A. 2019 Dec 18. pii: 1913690116. doi:, 10.1073/pnas.1913690116. PMID:31852826[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Trstenjak N, Milic D, Graewert MA, Rouha H, Svergun D, Djinovic-Carugo K, Nagy E, Badarau A. Molecular mechanism of leukocidin GH-integrin CD11b/CD18 recognition and species specificity. Proc Natl Acad Sci U S A. 2019 Dec 18. pii: 1913690116. doi:, 10.1073/pnas.1913690116. PMID:31852826 doi:http://dx.doi.org/10.1073/pnas.1913690116
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