Dynamic light scattering study of the two-domain structure ofHumicola insolensendoglucanase V

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Abstract
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 .