 |
PDBsum entry 1cel
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Hydrolase(o-glycosyl)
|
PDB id
|
|
|
|
1cel
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The three-Dimensional crystal structure of the catalytic core of cellobiohydrolase i from trichoderma reesei.
|
|
|
Authors
|
|
C.Divne,
J.Ståhlberg,
T.Reinikainen,
L.Ruohonen,
G.Pettersson,
J.K.Knowles,
T.T.Teeri,
T.A.Jones.
|
|
|
Ref.
|
|
Science, 1994,
265,
524-528.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Cellulose is the major polysaccharide of plants where it plays a predominantly
structural role. A variety of highly specialized microorganisms have evolved to
produce enzymes that either synergistically or in complexes can carry out the
complete hydrolysis of cellulose. The structure of the major cellobiohydrolase,
CBHI, of the potent cellulolytic fungus Trichoderma reesei has been determined
and refined to 1.8 angstrom resolution. The molecule contains a 40 angstrom long
active site tunnel that may account for many of the previously poorly understood
macroscopic properties of the enzyme and its interaction with solid cellulose.
The active site residues were identified by solving the structure of the enzyme
complexed with an oligosaccharide, o-iodobenzyl-1-thio-beta-cellobioside. The
three-dimensional structure is very similar to a family of bacterial
beta-glucanases with the main-chain topology of the plant legume lectins.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Crystallization and preliminary X-Ray studies on the core proteins of cellobiohydrolase i and endoglucanase i from trichoderma reesei.
|
|
|
Authors
|
|
C.Divne,
I.Sinning,
J.Ståhlberg,
G.Pettersson,
M.Bailey,
M.Siika-Aho,
E.Margolles-Clark,
T.Teeri,
T.A.Jones.
|
|
|
Ref.
|
|
J Mol Biol, 1993,
234,
905-907.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
