Structure of full-length bacterial chitinase containing two fibronectin type III domains revealed by small angle X-ray scattering.
Chitinase A1 (ChiA1) from Bacillus circulans WL-12 consists of an N-terminal catalytic domain, two fibronectin type III domains (FnIIIDs), and a C-terminal chitin-binding domain. The full-length structure of ChiA1 was studied by small angle X-ray scattering. The obtained low-resolution structure showed that ChiA1 is an elongated molecule with a length of approximately 145 A composed of a large globular head and a rod-like tail. Combination with known high-resolution structures of individual ChiA1 domains provided a model of the domain arrangement. In this model, two FnIIIDs connect to each other in an extended rod-like shape without large bending between the FnIIIDs, and contribute largely to the length of ChiA1.
Toratani
Tadayuki
T
Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University, 8050 Ikarashi-2, Niigata 950-2181, Japan.
Kezuka
Yuichiro
Y
Nonaka
Takamasa
T
Hiragi
Yuzuru
Y
Watanabe
Takeshi
T
D001407:Bacillus / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D002688:Chitinases / Q000737:chemistry* / Q000235:genetics; D005353:Fibronectins / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012542:Scattering, Radiation; D014965:X-Rays
D001426:Bacterial Proteins; D005353:Fibronectins; D011994:Recombinant Proteins; D002688:Chitinases; C094590:chitinase ChiA