Dynamic light scattering study of the two-domain structure of Humicola insolens endoglucanase V
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 sc...
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Published in | FEBS letters Vol. 376; no. 1; pp. 49 - 52 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier B.V
27.11.1995
Wiley |
Subjects | |
Online Access | Get full text |
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Summary: | 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
42 × 133.6
A
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(95)01244-0 |