Solution structure and conformational changes of the Streptomyces chitin-binding protein (CHB1)
Autor(en): | Svergun, DI Becirevic, A Schrempf, H Koch, MHJ Gruber, G |
Stichwörter: | ALPHA-CHITIN; Biochemistry & Molecular Biology; BIOPOLYMERS; CELLULOMONAS-FIMI; DIRECT SHAPE DETERMINATION; DOMAIN; GENE; NUCLEAR-MAGNETIC-RESONANCE; OLIVACEOVIRIDIS; SMALL-ANGLE-SCATTERING; TRYPTOPHAN RESIDUES | Erscheinungsdatum: | 2000 | Herausgeber: | AMER CHEMICAL SOC | Enthalten in: | BIOCHEMISTRY | Band: | 39 | Ausgabe: | 35 | Startseite: | 10677 | Seitenende: | 10683 | Zusammenfassung: | The shape and overall dimensions of the recently discovered Streptomyces alpha-chitin-binding protein, CHB 1, were investigated by synchrotron radiation X-ray solution scattering. The radius of gyration and the maximum size of CHB 1 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 CHB 1 depend strongly on the presence of disulfide bonds; upon their reduction, the protein loses its affinity to chitin. |
ISSN: | 00062960 | DOI: | 10.1021/bi000865p |
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geprüft am 06.06.2024