EC Number   |
|---|
   3.4.21.62 | - |
| 3.4.21.62 | 1.8 A resolution structure of an inactive form (by replacing the catalytic nucleophile Ser 221 with alanine) of the protease subtilisin S189, in complex with azide and with a prodomain substrate that spans the active site. The substrate is well ordered across the active site, and the azide anion is observed bound adjacent to Ala 32. Although S189, like wild-type subtilisin, has Ser as the catalytic nucleophile at residue 221, these crystal structures have Ala 221 to prevent cleavage of the substrate |
| 3.4.21.62 | a comparative study of psychrophilic, mesophilic and thermophilic subtilisin-like serine proteases by all-atom molecular dynamics simulations is performed. The thermophilic subtilisin presents a high affinity calcium binding site which is not structurally conserved in the mesophilic and psychrophilic counterparts, which at the same position show a stable salt bridge network and no stabilizing intra-molecular interactions, respectively |
| 3.4.21.62 | at 1.4 A resolution |
| 3.4.21.62 | by sitting-drop, vapor-diffusion method. Crystal structures of the autoprocessed/unautoprocessed form and mature forms of subtilisin at 1.89 A and 1.70 A resolution, respectively. Crystals show a unique Ca2+-binding site and that the N-terminal region of the mature domain (Gly70ΒPro82), which binds tightly to the main body in the unautoprocessed form, is disordered and mostly truncated in the autoprocessed and mature forms, respectively. Crystal structure of the propeptide:S324A-subtilisin complex at 1.65 a resolution |
| 3.4.21.62 | by the batch method from buffer solution saturated with Na2SO4 ca. 13% (w/v) as precipitant. Placement of several Cs+ and Cl- ions in crystals of subtilisin Carlsberg. The protein conformation is very similar to that of the enzyme without CsCl in acetonitrile. 11 defined sites for Cs+ cations and 8 Cl- anions around the protein molecule, although most of these have partial occupancy and may represent nonspecific binding sites. Two Cs+ and two Cl- ions are close to the mouth of the active site cleft, where they may affect catalysis. CsCl-treated subtilisin crystals transferred to acetonitrile show catalytic activity several fold higher than the reference crystals containing Na+ |
| 3.4.21.62 | by the hanging drop vapor-diffusion method, at 0.8 A resolution. Crystals belong to the monoclinic space group P21. Unit cell parameters are a = 46.09 A, b = 62.67 A, c = 84.87 A, and beta = 95.5°, indicating two molecules of Sph in the asymmetric unit. The crystal structures of the psychrophilic Bacillus TA41 subtilisin S41 and the mesophilic subtilisin Sph are nearly identical with the same calcium-loaded state in that five calcium ions are bound to each protein molecule |
| 3.4.21.62 | by the hanging drop vapor-diffusion method, at 1.4 A resolution. Crystals belong to either the tetragonal space group P41212 or P43212. Unit cell dimensions are a = b = 61 A and c = 174.77 A , indicating one monomer in the asymmetric unit. The crystal structures of the psychrophilic subtilisin S41 and the mesophilic Bacillus sphaericus subtilisin Sph are nearly identical with the same calcium-loaded state in that five calcium ions are bound to each protein molecule |
| 3.4.21.62 | by the hanging-drop vapour-diffusion method. Crystals of AprB2 diffract to 1.7 A resolution. The crystals belong to space group P1, with unit-cell parameters a = 42.7, b = 45.8, c = 45.7 A , alpha = 98.4, beta = 114.0, gamma = 114.6. The crystals contain one molecule in the asymmetric unit, with a solvent content of 36% |
| 3.4.21.62 | by the hanging-drop vapour-diffusion method. Crystals of AprV2 diffract to 2.0 A resolution. The crystals belong to space group P1, with unit-cell parameters a = 43.1, b = 46.0, c = 47.2 A , alpha = 97.8, beta = 115.2, gamma = 115.2. The crystals contain one molecule in the asymmetric unit, with a solvent content of ca. 36% |
