EC Number   |
|---|
   3.1.1.74 | - |
| 3.1.1.74 | crystal structures of S226P mutant in the Ca2+-bound and free states at 1.75 and 1.45 A resolution, respectively. A Ca2+ ion is coordinated by four residues within loop regions (the Ca2+ site) and two water molecules in a tetragonal bipyramidal array. The binding of Ca2+ induces large conformational changes in three loops, accompanied by the formation of additional interactions. The binding of Ca2+ stabilizes a region that is flexible in the Ca2+-free state but also modifies the substrate-binding groove by stabilizing an open conformation that allows the substrate to bind easily |
| 3.1.1.74 | crystallization and preliminary X-ray analysis of cutinase-inhibitor complexes, resolution beyond 1.6 A |
| 3.1.1.74 | crystallization of native enzyme, 27 mutant enzymes and 4 covalently inhibited complexes, crystallizes in 8 different crystal forms |
| 3.1.1.74 | hanging drop vapor diffusion method at 20°C, crystal structure of the inactive form of a Cut190 mutant, S226P/R228S/S176A, in complex with calcium ions and/or substrates |
| 3.1.1.74 | homology modeling of structure |
| 3.1.1.74 | in the absence and in the presence of the inhibitors diethyl p-nitrophenyl phosphate (belongs to space group P21) and 3-phenethylthio-1,1,1-trifluoropropan-2-one (belongs to space group P212121), to resolutions of 2.6 and 2.3 A, respectively. Apo-cutinase, 1.9 A resolution, belongs to space group P41212 with one subunit in the asymmetric unit with unit cell parameters a = 60, b = 60, c = 86 A, respectively. The catalytic triad (Ser136, Asp191, and His204) adopts an unusual configuration with the putative essential histidine His204 swung out of the active site into a position where it is unable to participate in catalysis, with the imidazole ring 11 A away from its expected position |
| 3.1.1.74 | modeling of structure |
| 3.1.1.74 | molecular dynamics simulations. The enzyme possesses a lid covering its active site and it is easier to open for the lid under an acidic pH condition. The binding of long-chain triglyceride is more stable at lower pH than higher pH |
| 3.1.1.74 | PDB ID 2CZQ, X-ray diffraction structure determination at 1.05 A resolution |
