Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei.
The enzymatic degradation of cellulose is an important process, both ecologically and commercially. The three-dimensional structure of a cellulase, the enzymatic core of CBHII from the fungus Trichoderma reesei reveals an alpha-beta protein with a fold similar to but different from the widely occurring barrel topology first observed in triose phosphate isomerase. The active site of CBHII is located at the carboxyl-terminal end of a parallel beta barrel, in an enclosed tunnel through which the cellulose threads. Two aspartic acid residues, located in the center of the tunnel are the probable catalytic residues.
Rouvinen
J
J
Department of Molecular Biology, BMC, Uppsala, Sweden.
Bergfors
T
T
Teeri
T
T
Knowles
J K
JK
Jones
T A
TA
D000595:Amino Acid Sequence; D001665:Binding Sites; D002482:Cellulose / Q000378:metabolism; D043366:Cellulose 1,4-beta-Cellobiosidase; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003460:Crystallization; D003461:Crystallography; D006026:Glycoside Hydrolases / Q000378:metabolism; D006031:Glycosylation; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D003904:Mitosporic Fungi / Q000201:enzymology*; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011487:Protein Conformation; D014242:Trichoderma / Q000201:enzymology*
D002482:Cellulose; D006026:Glycoside Hydrolases; D043366:Cellulose 1,4-beta-Cellobiosidase