Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii.

@article{Grassick2004ThreedimensionalSO,
  title={Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii.},
  author={A. Grassick and P. Murray and R{\'o}isı́n Thompson and C. Collins and L. Byrnes and G. Birrane and T. Higgins and M. Tuohy},
  journal={European journal of biochemistry},
  year={2004},
  volume={271 22},
  pages={
          4495-506
        }
}
The X-ray structure of native cellobiohydrolase IB (CBH IB) from the filamentous fungus Talaromyces emersonii, PDB 1Q9H, was solved to 2.4 A by molecular replacement. 1Q9H is a glycoprotein that consists of a large, single domain with dimensions of approximately 60 A x 40 A x 50 A and an overall beta-sandwich structure, the characteristic fold of Family 7 glycosyl hydrolases (GH7). It is the first structure of a native glycoprotein and cellulase from this thermophilic eukaryote. The long… Expand
Construction of thermostable cellobiohydrolase I from the fungus Talaromyces cellulolyticus by protein engineering.
Expression of Talaromyces emersonii cellobiohydrolase Cel7A in Saccharomyces cerevisiae and rational mutagenesis to improve its thermostability and activity.
A thermophilic endo-1,4-β-glucanase from Talaromyces emersonii CBS394.64 with broad substrate specificity and great application potentials
Loop variants of the thermophile Rasamsonia emersonii Cel7A with improved activity against cellulose
Two structurally discrete GH7-cellobiohydrolases compete for the same cellulosic substrate fiber
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 64 REFERENCES
Kinetic parameters and mode of action of the cellobiohydrolases produced by Talaromyces emersonii.
...
1
2
3
4
5
...