EC Number |
---|
4.2.2.2 | - |
4.2.2.2 | 1.6 A resolution crystal structure |
4.2.2.2 | crystal structure determined at 1.5 A resolution by the multiple isomorphous replacement method |
4.2.2.2 | crystal structure of PelI is solved to 1.45 A resolution. It consists of an N-terminal domain harboring a fibronectin type III fold linked to a catalytic domain displaying a parallel beta-helix topology. The N-terminal domain is located away from the active site and is not involved in the catalytic process. The structure of PelI in complex with its substrate, a tetragalacturonate, is solved to 2.3 A resolution. The sugar binds from subsites -2 to +2 in one monomer of the asymmetric unit, although it lies on subsites -1 to +3 in the other. These two Michaelis complexes are consistent with the dual mode of bond cleavage in this substrate. The bound sugar adopts a mixed 21 and 31 helical conformation similar to that reported in inactive mutants from families PL-1 and PL-10 |
4.2.2.2 | crystallization of mutant enzyme C132I/C156N/C194L, hanging-drop vapour-diffusion method |
4.2.2.2 | crystallographic analysis of 11 enzyme-Ca2+ complexes formed at pH 4.5, 9.5 and 11.2 under varying Ca2+ concentrations, solved and refined at a resolution of 2.2 A |
4.2.2.2 | crystals grown at pH 4.0, to 1.57 A resolution |
4.2.2.2 | hanging drop vapor diffusion method at 18°C, apo form (1.5 A resolution), a metal-bound form of YePL2A (2.0 A resolution) and a trigalacturonic acid-bound substrate complex (2.1 A resolution) |
4.2.2.2 | hanging-drop vapor-diffusion method, crystal structure of the PelA T1.5 mutant solved to 1.6 and 2.9 A resolution. Four residues in the T1.5 loop region of PelA are mutated (N215S, T217S, S219G and A220S) to match the structurally analogous T1.5 loop of PelE |
4.2.2.2 | hanging-drop vapour-diffusion method at 4°C. The crystals are hexagonal, with unit-cell parameters a = b = 85.55 A, c * 230.13 A, gamma = 120° and belong to space group P6(5)22 or P6(1)22, having one molecule per asymmetric unit |