4jmf
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jmf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JMF FirstGlance]. <br> | <table><tr><td colspan='2'>[[4jmf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JMF FirstGlance]. <br> | ||
| - | </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></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]] 2.099Å</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></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=4jmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jmf OCA], [https://pdbe.org/4jmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jmf RCSB], [https://www.ebi.ac.uk/pdbsum/4jmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jmf 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=4jmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jmf OCA], [https://pdbe.org/4jmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jmf RCSB], [https://www.ebi.ac.uk/pdbsum/4jmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jmf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/EXOT_PSEAE EXOT_PSEAE] Bifunctional effector protein that is secreted and delivered by the type III secretion system into eukaryotic target cells. The N-terminus encodes a GTPase-activating protein activity, whereas the C-terminus encodes an ADP-ribosyltransferase activity (PubMed:11298647). ADP-ribosylates several eukaryotic proteins including CT10 regulator of kinase (Crk) proteins (PubMed:12807879). In turn, induces atypical anoikis apoptosis by transforming Crk adaptor protein into a cytotoxin (PubMed:26020630). Affects host cell morphology by disrupting the actin cytoskeleton (PubMed:14688136). In addition to this activity, acts via its N-terminal region as a GTPase-activating protein (GAP) for host Rho GTPases including RhoA, Rac1, Cdc42 and Ras (PubMed:11895987). The GAP domain activity induces mitochondrial disruption in the target host cell by activating host caspases 3 and 9 that execute cellular death (PubMed:26451042). This activity also causes stress fiber disassembly (PubMed:11895987).<ref>PMID:11298647</ref> <ref>PMID:11895987</ref> <ref>PMID:12807879</ref> <ref>PMID:14688136</ref> <ref>PMID:26020630</ref> <ref>PMID:26451042</ref> | [https://www.uniprot.org/uniprot/EXOT_PSEAE EXOT_PSEAE] Bifunctional effector protein that is secreted and delivered by the type III secretion system into eukaryotic target cells. The N-terminus encodes a GTPase-activating protein activity, whereas the C-terminus encodes an ADP-ribosyltransferase activity (PubMed:11298647). ADP-ribosylates several eukaryotic proteins including CT10 regulator of kinase (Crk) proteins (PubMed:12807879). In turn, induces atypical anoikis apoptosis by transforming Crk adaptor protein into a cytotoxin (PubMed:26020630). Affects host cell morphology by disrupting the actin cytoskeleton (PubMed:14688136). In addition to this activity, acts via its N-terminal region as a GTPase-activating protein (GAP) for host Rho GTPases including RhoA, Rac1, Cdc42 and Ras (PubMed:11895987). The GAP domain activity induces mitochondrial disruption in the target host cell by activating host caspases 3 and 9 that execute cellular death (PubMed:26451042). This activity also causes stress fiber disassembly (PubMed:11895987).<ref>PMID:11298647</ref> <ref>PMID:11895987</ref> <ref>PMID:12807879</ref> <ref>PMID:14688136</ref> <ref>PMID:26020630</ref> <ref>PMID:26451042</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | ExoT belongs to the family of type 3 secretion system (T3SS) effector toxins in Pseudomonas aeruginosa, known to be one of the major virulence determinant toxins that cause chronic and acute infections in immuno-compromised individuals, burn victims and cystic fibrosis patients. Here, we report the X-ray crystal structure of the amino terminal fragment of effector toxin ExoT, in complex with full-length homodimeric chaperone SpcS at 2.1 A resolution. The full-length dimeric chaperone SpcS has the conserved alpha-beta-beta-beta-alpha-beta-beta-alpha fold of class I chaperones, the characteristic hydrophobic patches for binding effector proteins and a conserved polar cavity at the dimeric interface. The stable crystallized amino terminal fragment of ExoT consists of a chaperone binding domain and a membrane localization domain that wraps around the dimeric chaperone. Site-directed mutagenesis experiments and a molecular dynamics study complement each other in revealing Asn65, Phe67 and Trp88 as critical dimeric interfacial residues that can strongly influence the effector-chaperone interactions. DATABASE: The atomic coordinates and structure factors of ExoT-SpcS complex (code 4JMF) have been deposited in the Protein Data Bank Japan (PDBj), Institute for Protein Research, Osaka University. | ||
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| - | Interfacial residues of SpcS chaperone affects binding of effector toxin ExoT in Pseudomonas aeruginosa: novel insights from structural and computational studies.,Dey S, Datta S FEBS J. 2014 Jan 4. doi: 10.1111/febs.12704. PMID:24387107<ref>PMID:24387107</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4jmf" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Crystal structure of ExoT (residues 28 -77)- SpcS complex from Pseudomonas aeruginosa at 2.1 angstrom
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