4jmf: Difference between revisions
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==Crystal structure of ExoT (residues 28 -77)- SpcS complex from Pseudomonas aeruginosa at 2.1 angstrom== | |||
<StructureSection load='4jmf' size='340' side='right' caption='[[4jmf]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4jmf]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JMF FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">exoT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE]), SpcS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=4jmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jmf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jmf RCSB], [http://www.ebi.ac.uk/pdbsum/4jmf PDBsum]</span></td></tr> | |||
</table> | |||
<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. | |||
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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: Datta, S | |||
[[Category: Dey, S | ==See Also== | ||
*[[Exoenzyme|Exoenzyme]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Pseae]] | |||
[[Category: Datta, S]] | |||
[[Category: Dey, S]] | |||
[[Category: T3ss]] | [[Category: T3ss]] | ||
[[Category: Toxin-chaperone complex]] | [[Category: Toxin-chaperone complex]] | ||
[[Category: Type iii secretion system]] | [[Category: Type iii secretion system]] | ||
[[Category: Virulent effector]] | [[Category: Virulent effector]] | ||
