Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
Caffeine | two caffeine molecules bind to CrChi1 in subsites -1 to +1 in the substrate-binding domain, binding structure, overview | Clonostachys rosea |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clonostachys rosea | A9LI60 | - |
- |
Subunits | Comment | Organism |
---|---|---|
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 | Comment | Organism |
---|---|---|
CrChi1 | - |
Clonostachys rosea |
More | the enzyme is a family 18 chitinase | Clonostachys rosea |
General Information | Comment | Organism |
---|---|---|
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 |