Solution Structure and Conformational Changes of the Streptomyces Chitin-Binding Protein (CHB1)†Click to copy article linkArticle link copied!
Abstract
The shape and overall dimensions of the recently discovered Streptomyces α-chitin-binding protein, CHB1, were investigated by synchrotron radiation X-ray solution scattering. The radius of gyration and the maximum size of CHB1 were determined to be 1.75 ± 0.03 nm and 6.0 ± 0.2 nm, respectively. Using two independent ab initio approaches the low-resolution shape of the protein was found to consist of two domains, an elongated main globule with a length of about 4 nm and a foot-like domain of about 2 nm width. The structural and functional properties of CHB1 depend strongly on the presence of disulfide bonds; upon their reduction, the protein loses its affinity to chitin.
†
This research was supported by the Deutsche Forschungsgemeinschaft (Schr203/6-2; awarded to H.S.), by the International Association for the Promotion of Cooperation with Scientists from the Independent States of the Former Soviet Union (INTAS; to D.I S. and M.H.J.K.) Grant 96-1115, the EU Biotechnology Program Grant BIO4-CT97-2143 (to D.I.S.). G.G. was supported by the National Institutes of Health (Grant A1 22444).
‡
European Molecular Biology Laboratory.
§
Institute of Crystallography.
‖
Abteilung Angewandte Genetik der Mikroorganismen.
*
To whom correspondence should be addressed. Phone: +49/(0)541 969 3504. Fax: +49/(0)541 969 3503. E-mail: ggrueber@ biologie.uni-osnabrueck.de.
⊥
Abteilung Zoophysiologie.
#
University of Florida.
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