Characterization of the molecular chaperone ClpB from the pathogenic spirochaete Leptospira interrogans
Fig 1
Structural characteristics of ClpBLi used in this study.
(A) Comparison of the domain organization of ClpB from L. interrogans and E. coli. Bacterial ClpB proteins are composed of the following domains: N-terminal domain (ND), nucleotide binding domain 1 (NBD1), middle coiled-coil domain (MD), and nucleotide binding domain 2 (NBD2). The functions of the domains are indicated at the top. The amino acid residue numbers are shown for each chaperone and the amino acid sequence identity between ClpBEc and ClpBLi is indicated for each domain. (B) CD spectra of ClpBLi at 20°C (folded form) and 75°C (unfolded form) are shown. The CD signal was expressed as mean molar residue ellipticity (θ). (C) Temperature-induced changes in the CD signal at 222 nm for ClpBLi.