Crystal structure and substrate‐binding mode of cellulase 12A from Thermotoga maritima

@article{Cheng2011CrystalSA,
  title={Crystal structure and substrate‐binding mode of cellulase 12A from Thermotoga maritima},
  author={Ya-Shan Cheng and Tzu Ping Ko and Tzu-hui Wu and Yanhe Ma and Chun-Hsiang Huang and H. L. Lai and Andrew H.-J. Wang and Je-Ruei Liu and Rey Ting Guo},
  journal={Proteins: Structure},
  year={2011},
  volume={79}
}
Cellulases have been used in many applications to treat various carbohydrate‐containing materials. Thermotoga maritima cellulase 12A (TmCel12A) belongs to the GH12 family of glycoside hydrolases. It is a β‐1,4‐endoglucanase that degrades cellulose molecules into smaller fragments, facilitating further utilization of the carbohydrate. Because of its hyperthermophilic nature, the enzyme is especially suitable for industrial applications. Here the crystal structure of TmCel12A was determined by… 
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References

SHOWING 1-10 OF 33 REFERENCES
The X-ray crystal structure of the Trichoderma reesei family 12 endoglucanase 3, Cel12A, at 1.9 A resolution.
TLDR
The structure of the fungal family 12 enzyme presented here allows a complete structural characterization of the glycoside hydrolase-C clan and is exploited to improve initial multiple isomorphous replacement phasing, and subsequent structure refinement.
The structure of Rhodothermus marinus Cel12A, a highly thermostable family 12 endoglucanase, at 1.8 A resolution.
TLDR
The structural similarity between this cellulase and the mesophilic enzymes serves to highlight features that may be responsible for its thermostability, chiefly an increase in ion pair number and the considerable stabilisation of a mobile region seen in S. lividans CelB2.
Crystal complex structures reveal how substrate is bound in the -4 to the +2 binding sites of Humicola grisea Cel12A.
TLDR
Four new crystal structures of wild-type Humicola grisea Cel12A are solved in complexes formed by soaking with cellobiose, cellotetraose,cellopentaose, and a thio-linked cellottraose derivative (G2SG2) to shed light on the mechanism and function of GH 12 cellulases.
The Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 A resolution.
TLDR
The overall fold of the enzyme shows a remarkable similarity to that of family 11 xylanases, as previously predicted by hydrophobic clustering analysis.
Dimerisation and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A.
TLDR
Small-angle X-ray scattering analysis of RmCel12A showed that the enzyme forms a loosely associated antiparallel dimer in solution, which may target the enzyme to the antipar parallel polymer strands in cellulose.
Determination of the structure of an endoglucanase from Aspergillus niger and its mode of inhibition by palladium chloride.
TLDR
Based on this structural study, one can conclude that the palladium ion directly binds to and blocks the active site of EglA and thus inactivates the enzyme.
The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 A resolution.
TLDR
The active site architecture of the complex provides insight into the double-displacement mechanism of retaining glycoside hydrolases and also sheds light on the basis of the differences in specificity between family 12 cellulases and family 11 xylanases.
Characterization and Three-dimensional Structures of Two Distinct Bacterial Xyloglucanases from Families GH5 and GH12*
TLDR
The enzymes, Paenibacillus pabuli XG5 and Bacillus licheniformis XG12, both display open active center grooves grafted upon their respective (β/α)8 and β-jelly roll folds, in which the side chain decorations of xyloglucan may be accommodated.
Structural and biochemical studies of GH family 12 cellulases: improved thermal stability, and ligand complexes.
TLDR
The structural and biochemical studies of these related GH 12 enzymes, and their variants, have provided insight on how specific residues contribute to protein thermal stability and enzyme activity, which can serve as a structural toolbox for the design of Cel12A enzymes with specific properties and features suited to existing or new applications.
The Humicola grisea Cel12A enzyme structure at 1.2 Å resolution and the impact of its free cysteine residues on thermal stability
TLDR
The H. grisea enzyme was much more stable to irreversible thermal denaturation than the Trichoderma reesei enzyme, and the three cysteines in H.grisea Cel12A play an important role in the thermal stability of this protein, although they are not involved in a disulfide bond.
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