Crystal structure of copper-bound tyrosinase from Streptomyces castaneoglobisporus in complex with the caddie protein obtained by soaking in the hydroxylamine-containing solution for 2 h at 277 K

Catalytic mechanism of tyrosinase implied from the quinone formation on the Tyr98 residue of the caddie protein

MTVRKNQATLTADEKRRFVAAVLELKRSGRYDEFVRTHNEFIMSDTDSGERTGHRSPSFLPWHRRFLLDFEQALQSVDSS
VTLPYWDWSADRTVRASLWAPDFLGGTGRSTDGRVMDGPFAASTGNWPINVRVDSRTYLRRSLGGSVAELPTRAEVESVL
AISAYDLPPYNSASEGFRNHLEGWRGVNLHNRVHVWVGGQMATGVSPNDPVFWLHHAYVDKLWAEWQRRHPDSAYVPTGG
TPDVVDLNETMKPWNTVRPADLLDHTAYYTFDALEHHHHHH

MPEITRRRALTAAAAVAATASAAVTLAAPAASAAGHHEPAAPESFDEVYKGRRIQGRPAGGGAHHHEHGGGYEVFVDGVQ
LHVMRNADGSWISVVSH(DAH)DPVPTPRAAARAAVDELQGAPLLPFPANLEHHHHHH

MPEITRRRALTAAAAVAATASAAVTLAAPAASAAGHHEPAAPESFDEVYKGRRIQGRPAGGGAHHHEHGGGYEVFVDGVQ
LHVMRNADGSWISVVSHFDPVPTPRAAARAAVDELQGAPLLPFPANLEHHHHHH

PEG 3350, SODIUM NITRATE, HEPES, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K

TYR98 IN PROTEIN MELC WAS PARTIALLY HYDROXYLATED TO DAH.

ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY ?

tyrosinase, catalytic mechanism, OXIDOREDUCTASE-METAL BINDING PROTEIN complex

MTVRKNQATLTADEKRRFVAAVLELKRSGRYDEFVRTHNEFIMSDTDSGERTGHRSPSFLPWHRRFLLDFEQALQSVDSS
VTLPYWDWSADRTVRASLWAPDFLGGTGRSTDGRVMDGPFAAFTGNWPINVRVDSRTYLRRSLGGSVAELPTRAEVESVL
AISAYDLPPYNSASEGFRNHLEGWRGVNLHNRVHVWVGGQMATGVSPNDPVFWLHHAYVDKLWAEWQRRHPDSAYVPTGG
TPDVVDLNETMKPWNTVRPADLLDHTAYYTFDA

MPEITRRRALTAAAAVAATASAAVTLAAPAASAAGHHEPAAPESFDEVYKGRRIQGRPAGGGAHHHEHGGGYEVFVDGVQ
LHVMRNADGSWISVVSHYDPVPTPRAAARAAVDELQGAPLLPFPAN