Solution structure and conformational changes of the Streptomyces chitin-binding protein (CHB1).
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.
Svergun
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European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
Bećirević
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A
Schrempf
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Koch
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Grüber
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D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D002686:Chitin / Q000737:chemistry / Q000378:metabolism*; D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D004220:Disulfides / Q000737:chemistry / Q000378:metabolism; D047908:Intracellular Signaling Peptides and Proteins; D010084:Oxidation-Reduction; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012542:Scattering, Radiation; D012996:Solutions; D013050:Spectrometry, Fluorescence; D013302:Streptomyces / Q000737:chemistry*; D013329:Structure-Activity Relationship; D014965:X-Rays
D001426:Bacterial Proteins; C091405:CHB1 protein, Streptomyces; D002352:Carrier Proteins; D004220:Disulfides; D047908:Intracellular Signaling Peptides and Proteins; D012996:Solutions; D002686:Chitin; D003545:Cysteine