[HTML][HTML] Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis
Y Matoba, T Kumagai, A Yamamoto, H Yoshitsu… - Journal of Biological …, 2006 - ASBMB
At high resolution, we determined the crystal structures of copper-bound and metal-free
tyrosinase in a complex with ORF378 designated as a" caddie" protein because it assists
with transportation of two Cu (II) ions into the tyrosinase catalytic center. These structures
suggest that the caddie protein covers the hydrophobic molecular surface of tyrosinase and
interferes with the binding of a substrate tyrosine to the catalytic site of tyrosinase. The
caddie protein, which consists of one six-strandedβ-sheet and one α-helix, has no similarity …
tyrosinase in a complex with ORF378 designated as a" caddie" protein because it assists
with transportation of two Cu (II) ions into the tyrosinase catalytic center. These structures
suggest that the caddie protein covers the hydrophobic molecular surface of tyrosinase and
interferes with the binding of a substrate tyrosine to the catalytic site of tyrosinase. The
caddie protein, which consists of one six-strandedβ-sheet and one α-helix, has no similarity …