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Glycobiology vol 2 no 4 pp. 321-326, 1992
© 1992

research-article

The tertiary structure of endo-ß-1,4-glucanase B (CenB), a multidomain cellulase from the bacterium Cellulomonas fimi

Andreas Meinke1,2, Maria Schmuck3, Neil R. Gilkes1,4, Douglas G. Kilburn1, Robert C. Miller, Jr.1 and R. Antony J. Warren1

Department of Microbiology, University of British Columbia Vancouver, BC, V6T 1Z3, Canada
Institut für Biologie III der Universitat Freiburg. Schänzlestraße 1, D-7800 Freiburg i. Br., FRG
Institut für Physikalische Chemie der Universität Graz A-8100 Graz, Austria

4To whom correspondence should be addressed

Received on March 9, 1992; accepted on May 13, 1992

Endo-ß-1,4-glucanase B (CenB) is a large (110 kDa) extra-cellular enzyme from the cellulolytic bacterium Cellulomonas fimi. CenB contains five domains, including a typical C.fimi cellulose-binding domain, separated by distinctive linker polypeptides (Meinke et al., 1991b). X-ray scattering analyses show that CenB has a highly elongated shape resembling beads on a string. The sizes of the polypeptides produced by treatment of CenB with proteases, together with their N-terminal amino acid sequences, show that at least two of the four linkers connecting the five domains of CenB are more sensitive to proteolysis than the domains themselves. It is concluded that the beads represent the domains of CenB, the string represents the linkers.

cellulase Cellulomonas cellulose-binding domain glucanase X-ray scattering


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