EC Number   |
|---|
   1.16.3.4 | 1.7 A resolution structure of a crystal soaked in CuCl2. A Cu(II) ion is bound to the protein 7.5 A from the T1 copper site in a region rich in methionine residues. The trigonal bipyramidal coordination sphere contains two methionine sulfur atoms, two aspartate carboxylate oxygen atoms, and a water molecule. Asp439 both ligates the labile copper and hydrogen-bonds to His443, which ligates the T1 copper. The type 3 copper atoms of the trinuclear cluster in the structure are bridged by a chloride ion that completes a square planar coordination sphere for the T2 copper atom |
| 1.16.3.4 | hanging drop method, crystal structure of CueO at 1.1 A with the 45-residue methionine-rich segment fully resolved, revealing an N-terminal helical segment with methionine residues juxtaposed for Cu(I) ligation and a C-terminal highly mobile segment rich in methionine and histidine residues. Structures of CueO with a C500S mutation, and CueO with six methionines changed to serine |
| 1.16.3.4 | structure at 1.1 A with the 45-residue methionine-rich segment fully resolved, revealing an N-terminal helical segment with methionine residues juxtaposed for Cu(I) ligation and a C-terminal highly mobile segment rich in methionine and histidine residues. Structures of mutant C500S and CueO with six methionines changed to serine. Soaking C500S CueO crystals with Cu(I), or wild-type CueO crystals with Ag(I), leads to occupancy of the substrate-binding site and two new sites along the methionine-rich helix, involving methionines 358, 362, 368, and 376 |
| 1.16.3.4 | structure of G304K mutant at 1.49 A resolution. The mutant shows dramatic conformational changes in methionine-rich helix and the relative regulatory loop. In the structure of Cu-soaked enzyme, the addition of Cu ions induces further conformational changes in the regulatory loop and methionine-rich helix as a result of the new Cu-binding sites on the enzyme's surface |
| 1.16.3.4 | structure of the region Pro357-His406 deletion mutant, to 1.81 A resolution |
| 1.16.3.4 | the acetate-bound form of the type II copper is found in the X-ray structure of CueO crystallized in acetate buffer in addition to the conventional OH(-)-bound form as the major resting form. When CueO is crystallized in citrate buffer, the OH(-)-bound form is present exclusively |
| 1.16.3.4 | to 1.4 A resolution. The overall structure is similar to those of laccase and ascorbate oxidase, but contains an extra 42-residue insert in domain 3 that includes 14 methionines, nine of which lie in a helix that covers the entrance to the type I copper site. In the trinuclear copper cluster the Cu-O-Cu binuclear species is nearly linear (Cu-O-Cu bond angle is 170°) and the third (type II) copper lies only 3.1 A from the bridging oxygen |
