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Literature summary extracted from

  • Yang, J.; Gan, Z.; Lou, Z.; Tao, N.; Mi, Q.; Liang, L.; Sun, Y.; Guo, Y.; Huang, X.; Zou, C.; Rao, Z.; Meng, Z.; Zhang, K.Q.
    Crystal structure and mutagenesis analysis of chitinase CrChi1 from the nematophagous fungus Clonostachys rosea in complex with the inhibitor caffeine (2010), Microbiology, 156, 3566-3574.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.14 purified enzyme CrChi1 free or in complex with inhibitor caffeine, hanging drop vapour diffusion method, 0.0005 ml protein solution, containing 20 mg/ml in 20 mM Tris/HCl, pH 8.0, and 0.0005 ml reservoir solution are mixed and equilibrated against 0.2 ml reservoir solution consisting of 0.2 M ammonium dihydrogen phosphate, and 15% w/v PEG3350, for the enzyme complex addition of 0.001 ml of 1 mM caffeine solution, 16°C, X-ray diffraction structure determination and analysis at 1.8 A and 1.6 A, respectively, molecular replacement Clonostachys rosea

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.14 Caffeine two caffeine molecules bind to CrChi1 in subsites -1 to +1 in the substrate-binding domain, binding structure, overview Clonostachys rosea

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.14 Clonostachys rosea A9LI60
-
-

Subunits

EC Number Subunits Comment Organism
3.2.1.14 More CrChi1 has the DXDXE motif at the end of strand beta5, with Glu174 as the catalytic residue in the middle of the open end of the (beta/alpha)8 barrel Clonostachys rosea

Synonyms

EC Number Synonyms Comment Organism
3.2.1.14 CrChi1
-
 Clonostachys rosea
3.2.1.14 More the enzyme is a family 18 chitinase Clonostachys rosea

General Information

EC Number General Information Comment Organism
3.2.1.14 physiological function chitinases are a group of enzymes capable of hydrolysing the bta-(1,4)-glycosidic bonds of chitin, an essential component of the fungal cell wall, the shells of nematode eggs, and arthropod exoskeletons Clonostachys rosea