4JMF

Crystal structure of ExoT (residues 28 -77)- SpcS complex from Pseudomonas aeruginosa at 2.1 angstrom

Summary for 4JMF

• Entry DOI: 10.2210/pdb4jmf/pdb
• Descriptor: Exoenzyme T, Probable chaperone, GLYCEROL, ... (4 entities in total)
• Functional Keywords: type iii secretion system, t3ss, virulent effector, toxin-chaperone complex, toxin/chaperone
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 3
• Total formula weight: 31852.04

Authors

Datta, S.,Dey, S. (deposition date: 2013-03-14, release date: 2014-02-05, Last modification date: 2024-03-20)

Primary citation

Dey, S.,Datta, S.
Interfacial residues of SpcS chaperone affects binding of effector toxin ExoT in Pseudomonas aeruginosa: novel insights from structural and computational studies
Febs J., 281:1267-1280, 2014

PubMed Abstract: 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 Å resolution. The full-length dimeric chaperone SpcS has the conserved α-β-β-β-α-β-β-α 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.

PubMed: 24387107
DOI: 10.1111/febs.12704

Experimental method

X-RAY DIFFRACTION (2.099 Å)