Abstract
The shape and overall dimensions of the recently discovered Streptomyces alpha-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.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Bacterial Proteins / chemistry*
-
Bacterial Proteins / isolation & purification
-
Bacterial Proteins / metabolism
-
Carrier Proteins / chemistry*
-
Carrier Proteins / isolation & purification
-
Carrier Proteins / metabolism
-
Chitin / chemistry
-
Chitin / metabolism*
-
Cysteine / chemistry
-
Cysteine / metabolism
-
Disulfides / chemistry
-
Disulfides / metabolism
-
Intracellular Signaling Peptides and Proteins
-
Oxidation-Reduction
-
Protein Binding
-
Protein Conformation
-
Protein Structure, Tertiary
-
Scattering, Radiation
-
Solutions
-
Spectrometry, Fluorescence
-
Streptomyces / chemistry*
-
Structure-Activity Relationship
-
X-Rays
Substances
-
Bacterial Proteins
-
CHB1 protein, Streptomyces
-
Carrier Proteins
-
Disulfides
-
Intracellular Signaling Peptides and Proteins
-
Solutions
-
Chitin
-
Cysteine