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SAXS Data Based Global Shape Analysis of Trigger Factor (TF) Proteins from E. coli, V. cholerae, and P. frigidicola: Resolving the Debate on the Nature of Monomeric and Dimeric Forms.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title SAXS Data Based Global Shape Analysis of Trigger Factor (TF) Proteins from E. coli, V. cholerae, and P. frigidicola: Resolving the Debate on the Nature of Monomeric and Dimeric Forms.
 
Creator Rathore, Yogendra S
Dhoke, Reema R
Badmalia, Maulik
Sagar, Amin
Ganguly, Ashish
 
Subject QR Microbiology
 
Description Dimerization of bacterial chaperone trigger factor (TF) is an inherent protein concentration based property which available biophysical characterization and crystal structures have kept debatable. We acquired small-angle X-ray scattering (SAXS) intensity data from different TF homologues from Escherichia coli (ECTF), Vibrio cholerae (VCTF), and Psychrobacter frigidicola (PFTF) while varying each protein concentration. We found that ECTF and VCTF adopt a compact dimeric shape at higher concentrations which did not resemble the "back-to-back" conformation reported earlier for ECTF from crystallography (PDB ID: 1W26 ). In contrast, PFTF remained monomeric throughout the concentration range 2-90 μM displaying a multimodal open extended conformation. OLIGOMER analysis showed that both the ECTF and VCTF remained completely monomeric at lower concentrations (2-11 μM), while, at higher concentrations (60-90 μM), they adopted a dimeric form. Interestingly, the equilibrium existed in the medium concentration range (>11 and
 
Publisher ACS Publications
 
Date 2015-05-21
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/1634/1/ashishrathore2015.pdf
Rathore, Yogendra S and Dhoke, Reema R and Badmalia, Maulik and Sagar, Amin and Ganguly, Ashish (2015) SAXS Data Based Global Shape Analysis of Trigger Factor (TF) Proteins from E. coli, V. cholerae, and P. frigidicola: Resolving the Debate on the Nature of Monomeric and Dimeric Forms. The journal of physical chemistry. B, 119 (20). pp. 6101-12. ISSN 1520-5207
 
Relation http://pubs.acs.org/doi/abs/10.1021/acs.jpcb.5b00759
http://crdd.osdd.net/open/1634/