Dynamic light scattering study of the two‐domain structure of Humicola insolens endoglucanase V

FEBS Letters

Schülein, Martin²  Henrissat, Bernard¹  Borsali, Redouane¹  Boisset, Claire¹ 

[1]Centre de Recherches sur les Macromolécules Végétales, CNRS, BP 53, F-38041 Grenoble cedex 9, France

[2]Novo-Nordisk als, Novo Allé, DK-2880 Bagsvaerd, Denmark

关键词: Cellulase;    Humicola insolens;    Endoglucanase;    Domain structure;    Dynamic light scattering;   

DOI  :  10.1016/0014-5793(95)01244-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Endoglucanase V (EG V) of Humicola insolens is composed of a catalytic domain and of a cellulose-binding domain linked by a 33 amino acid long peptide rich in Ser, Thr and Pro residues. This work describes the dynamic behavior of the two-domain structure of EG V as revealed by quasi-elastic light scattering experiments. For both the full-length and the isolated catalytic domain, the autocorrelation function is essentially described by a single relaxation mode. The equivalent hydrodynamic radius of the catalytic domain was found to correspond precisely to the dimensions measured from the previously determined three-dimensional structure. The results obtained with the full-length protein allow a description of the two domain structure of EG V similar to that resulting from earlier studies using small angle X-ray scattering on cellulases from Trichoderma reesei. The hydrodynamic dimensions of the entire enzyme can be approximated as an ellipsoid with dimensions of .

【 授权许可】

Unknown