Crystal structure of a glycoside hydrolase family 6 enzyme, CcCel6C, a cellulase constitutively produced by Coprinopsis cinerea

@article{Liu2010CrystalSO,
  title={Crystal structure of a glycoside hydrolase family 6 enzyme, CcCel6C, a cellulase constitutively produced by Coprinopsis cinerea},
  author={Yuan Liu and Makoto Yoshida and Yuma Kurakata and Takatsugu Miyazaki and Kiyohiko Igarashi and Masahiro Samejima and Kiyoharu Fukuda and Atsushi Nishikawa and Takashi Tonozuka},
  journal={The FEBS Journal},
  year={2010},
  volume={277}
}
The basidiomycete Coprinopsis cinerea produces the glycoside hydrolase family 6 enzyme CcCel6C at low and constitutive levels. CcCel6C exhibits unusual cellobiohydrolase activity; it hydrolyses carboxymethyl cellulose, which is a poor substrate for typical cellobiohydrolases. Here, we determined the crystal structures of CcCel6C unbound and in complex with p‐nitrophenyl β‐d‐cellotrioside and cellobiose. CcCel6C consists of a distorted seven‐stranded β/α barrel and has an enclosed tunnel, which… 
Comparison of the structural changes in two cellobiohydrolases, CcCel6A and CcCel6C, from Coprinopsis cinerea – a tweezer‐like motion in the structure of CcCel6C
TLDR
The crystal structures of the CcCel6A catalytic domain complexed with a Hepes buffer molecule, with cellobiose, and with p‐nitrophenyl β‐d‐cellotrioside (pNPG3) are determined.
The structure of a bacterial cellobiohydrolase: the catalytic core of the Thermobifida fusca family GH6 cellobiohydrolase Cel6B.
TLDR
The enzyme structure reveals that the Cel6B enzyme has a much longer substrate-binding site than its fungal GH6 counterparts, and the tunnel is comparable in length to that of GH7 CBHs.
Crystal structures of the GH6 Orpinomyces sp. Y102 CelC7 enzyme with exo and endo activity and its complex with cellobiose.
TLDR
LC-MS/MS analysis revealed cellobiose (major) and cellotriose (minor) to be the respective products of endo and exo activity of the GH6 Orp CelC7.
Crystal structure of the N‐terminal domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea
TLDR
The crystal structure of the N‐terminal putative catalytic domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea was determined and it was suggested that the catalytic mechanism of CcGH131A is different from that of typical glycosidases.
X-ray structure and function studies of key enzymes for biomass conversion: GH6 cellobiohydrolases and GH61 lytic polysaccharide monooxygenases (LPMO)
The need for large enzyme quantities due to the difficult hydrolysis of recalcitrant polysaccharides is still a major barrier to economical biomass conversion for biofuel production. To discover or
A mutation in an exoglucanase of Xanthomonas oryzae pv. oryzae, which confers an endo mode of activity, affects bacterial virulence, but not the induction of immune responses, in rice.
TLDR
D131A CbsA was as proficient as wild-type (Wt) CBSA in inducing rice immune responses, but was deficient in virulence-promoting activity, which indicates that the specific exoglucanase activity of the Wt Cbs a protein is required for this protein to promote the growth of Xoo in rice.
Insight into the process of product expulsion in cellobiohydrolase Cel6A from Trichoderma reesei by computational modeling
TLDR
Conventional molecular dynamics and steered molecular dynamics (SMD) were applied to study product expulsion from TrCel6A and found that Tyr103 may be a crucial residue in product expulsion given that it exhibits two different posthydrolytic conformations.
Characterization of the Wild-Type and Truncated Forms of a Neutral GH10 Xylanase from Coprinus cinereus: Roles of C-Terminal Basic Amino Acid-Rich Extension in Its SDS Resistance, Thermostability, and Activity.
A neutral xylanase (CcXyn) was identified from Coprinus cinereus. It has a single GH10 catalytic domain with a basic amino acid-rich extension (PVRRK) at the C-terminus. In this study, the wild-type
Molecular Cloning and Expression of a Family 6 Cellobiohydrolase Gene cbhII from Penicillium funiculosum NCL1
TLDR
The recombinant cellobiohydrolase produced by P. pastoris (pPICBH6) showed maximum activity at pH 4.0 and temperature 50&degC and higher specificity in hydrolysis of filter-paper.
Molecular Cloning and Expression of a Family 6 Cellobiohydrolase Gene cbhII from Penicillium funiculosum NCL 1
Aim: Lignocelluloytic enzymes are the largest class of hydrolase enzyme which utilizes the plant biomass to produce renewable sources. Hence practices for larger production of these enzymes at lower
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References

SHOWING 1-10 OF 44 REFERENCES
Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 A resolution.
TLDR
The structure of the catalytic core of the family 6 endoglucanase Cel6B from Humicola insolens has been solved by molecular replacement with the known T. reesei cellobiohydrolase II as the search model and reveals that the deletion of just a single loop of the active site peels open the active-site tunnel to reveal a substrate-binding groove.
Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding.
TLDR
The structure of the catalytic core domain of Humicola insolens cellobiohydrolase II Cel6A in complex with glucose/cellotetraose provides the first three-dimensional demonstration of conformational change in this class of enzymes.
Family 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 A resolution and homology models of the isozymes.
TLDR
The results suggest that at least two of the five other family 7 genes found in P. chrysosporium will have differences in specificity and possibly catalytic mechanism, thus offering some explanation for the presence of Cel7 isozymes in this species, which are differentially expressed in response to various growth conditions.
The active site of Trichoderma reesei cellobiohydrolase II: the role of tyrosine 169.
TLDR
Data suggest that Y169, on interacting with a glucose ring entering the second subsite in a narrow tunnel, helps to distort the glucose ring into a more reactive conformation, and catalytic constants towards cellotriose and cellotetraose are four times lower for the mutant.
Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion.
TLDR
The structure of the catalytic domain of Cel6A from T. fusca in complex with a nonhydrolysable substrate analogue that acts as an inhibitor, methylcellobiosyl-4-thio-beta- cellobioside (Glc(2)-S-GlC(2), has been determined to 1.5 A resolution.
Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A resolution.
TLDR
There is no crystallographic evidence in the present structure to support a mechanism involving loop opening, yet preliminary modelling experiments suggest that the active-site tunnel of Cel6A (CBH II) is too narrow to permit entry of a fluorescenyl-derivatized substrate, known to be a viable substrate for this enzyme.
Cloning and Transcript Analysis of Multiple Genes Encoding the Glycoside Hydrolase Family 6 Enzyme from Coprinopsis cinerea
TLDR
Five genes encoding the glycoside hydrolase family 6 (GH6) enzyme are found in the genome database of the basidiomycete Coprinopsis cinerea and the amino acid sequence of CcCel6A suggests a two-domain structure consisting of an N-terminal family 1 carbohydrate-binding module (CBM1) and a GH6 catalytic domain.
Heterologous expression, crystallization and preliminary X-ray characterization of CcCel6C, a glycoside hydrolase family 6 enzyme from the basidiomycete Coprinopsis cinerea.
TLDR
Here, the crystallization of CcCel6C produced in Escherichia coli is reported, and the square prismatic crystal belonged to the triclinic space group P1, with unit-cell parameters a = 44.04, b = 45.04 and c = 48.11.
The active site of cellobiohydrolase Cel6A from Trichoderma reesei: the roles of aspartic acids D221 and D175.
TLDR
Site-directed mutagenesis, X-ray crystallography, and enzyme kinetic studies have been used to confirm the role of residue D221 as the catalytic acid in Cel6A, and suggest that the single-displacement mechanism of Cel 6A may not directly involve a catalytic base.
Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Ce16A from trichoderma reesei.
TLDR
The crystallographic results show that one of the tunnel-forming loops in Cel6A is sensitive to modifications at the active site, and is able to take on a number of different conformations.
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