EC Number   |
|---|
   1.14.99.53 | homology modeling, CbpD is a monomeric tri-modular enzyme with flexible linkers |
| 1.14.99.53 | homology modeling. Residues His1 and His61 directly coordinate the basic copper cofactor in T-shaped geometry. The axial, noncoordinating active site residue is Tyr142 |
| 1.14.99.53 | in presence of Zn2+, to 1.55 A resolution, and in presence of Cu2+, to 1.4 AS resolution |
| 1.14.99.53 | molecular dynamics interactions between the LPMO and three different surface topologies of crystalline chitin. Most enzyme-substrate interactions involve the polysaccharide chain that is to be cleaved. Enzyme displays a constrained active site geometry as well as a tunnel connecting the bulk solvent to the copper site, through which only small molecules such as H2O, O2, and H2O2 can diffuse. Rearrangement of Cu-coordinating water molecules is necessary when binding the substrate and also provide a rationale for the experimentally observed C1 oxidative regiospecificity |
| 1.14.99.53 | solution-phase structure of apo-LPMO10A and of Cu(I)-LPMO10A. The presence of the metal has minimal effects on the overall protein structure. Large changes in the Cu(II) spin-Hamiltonian parameters are induced upon binding of the substrate. Changes arise from a rearrangement of the copper coordination sphere from a five-coordinate distorted square pyramid to a four-coordinate near-square planar |
| 1.14.99.53 | structure of the catalytic domain (residues 37-230, lacking the linker and the CBM2) to 1.08 A resolution. Structure shows the typical LPMO fold with a central beta-sandwich made up by two distorted beta-sheets connected by several loops and helices. The active site is formed by His37 and His144 that coordinate the copper atom in a T-shaped geometry |
| 1.14.99.53 | structure of the catalytic domain, residues 37-230, to 1.08 A resolution. The active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry |
| 1.14.99.53 | structure shows a substrate-binding surface with features similar to known chitin-active LPMOs and the absence of a carbohydrate-binding module |
| 1.14.99.53 | structures in the resting state and of a copper(II)-dioxo intermediate complex formed in the absence of substrate reveal pre-bound molecular oxygen adjacent to the active site. A conserved histidine is involved in promoting oxygen activation |
| 1.14.99.53 | to 1.2 A resolution. Diffraction resolution and crystal morphology are improved by expression from a glycoengineered strain of Pichia pastoris |
