The tertiary structure of endo-beta-1,4-glucanase B (CenB), a multidomain cellulase from the bacterium Cellulomonas fimi.
Endo-beta-1,4-glucanase B (CenB) is a large (110 kDa) extracellular 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.
Meinke
A
A
Department of Microbiology, University of British Columbia, Vancouver, Canada.
Schmuck
M
M
Gilkes
N R
NR
Kilburn
D G
DG
Miller
R C
RC
Warren
R A
RA
D000192:Actinomycetales / Q000201:enzymology*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002480:Cellulase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D002482:Cellulose / Q000378:metabolism; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002918:Chymotrypsin / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010206:Papain / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism
D010446:Peptide Fragments; D002482:Cellulose; D002480:Cellulase; D010450:Endopeptidases; D002918:Chymotrypsin; D010206:Papain