Interfacial residues of SpcS chaperone affects binding of effector toxin ExoT in Pseudomonas aeruginosa: novel insights from structural and computational studies
Article first published online: 23 JAN 2014
© 2014 FEBS
Volume 281, Issue 4, pages 1267–1280, February 2014
How to Cite
Dey, S. and Datta, S. (2014), Interfacial residues of SpcS chaperone affects binding of effector toxin ExoT in Pseudomonas aeruginosa: novel insights from structural and computational studies. FEBS Journal, 281: 1267–1280. doi: 10.1111/febs.12704
- Issue published online: 17 FEB 2014
- Article first published online: 23 JAN 2014
- Accepted manuscript online: 4 JAN 2014 06:55AM EST
- Manuscript Accepted: 23 DEC 2013
- Manuscript Revised: 6 DEC 2013
- Manuscript Received: 30 SEP 2013
- Department of Science and Technology and Council of Scientific and Industrial Research, Government of India
Fig. S1. Mass spectrometry from ExoT–SpcS crystal.
Fig. S2. Chaperone–chaperone and chaperone–effector interactions.
Fig. S3. Overview of in silico alanine scanning mutagenesis binding data.
Fig. S4. Root mean square deviation and superposition of time-averaged structures of SpcS wild-type and mutants obtained from molecular dynamics simulation.
Fig. S5. Root mean square fluctuations for Cα atoms of the chaperone backbone, averaged over the time course of the simulation.
Fig. S6. Sensograms from surface plasmon resonance assay of ExoT–SpcS interaction.
Fig. S7. Far UV and near UV CD spectroscopy of wild-type and double SpcS mutants.
Fig. S8. Superimposition of chaperones SycE and SpcS, in the absence and presence of YopE and ExoT effectors, respectively.
Table S1. Details of residue contact existing between two dimeric chaperones.
Table S2. Details of residue contact existing between dimeric chaperone and effector.
Table S3. Summary of in silico alanine scanning mutations with their corresponding ΔΔGbind values.
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