Crystal structure of the LnmA cytochrome P450 hydroxylase from the leinamycin biosynthetic pathway of Streptomyces atroolivaceus S-140 at 1.9 A resolution

Midwest Center for Structural Genomics (MCSG)

Enzyme Discovery for Natural Product Biosynthesis (NatPro)

Crystal structure of the LnmA cytochrome P450 hydroxylase from the leinamycin biosynthetic pathway of Streptomyces atroolivaceus S-140

0.2 M ammonium acetate, 0.1 M Bis-Tris, pH 6.77, 25% PEG3350, VAPOR DIFFUSION, SITTING DROP

Enzyme Discovery for Natural Product Biosynthesis

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

National Institutes of Health/National Cancer Institute (NIH/NCI)

THE CONSTRUCT WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG MGSSHHHHHHSQDPGDENLYFQS. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A SERINE (0) FOLLOWED BY THE TARGET SEQUENCE.

1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT. 4. THE HEME IRON IS MODELED AS FE2+ AND IS LIKELY REDUCED BY X-RAY EXPOSURE. 5. A PEG FRAGMENT FROM THE CRYSTLLIZATOION CONDITIONS HAVE BEEN MODELED.

hydroxylase, leinamycin, heme, monooxygenase, OXIDOREDUCTASE, Structural Genomics, PSI-Biology, Midwest Center for Structural Genomics, MCSG, Enzyme Discovery for Natural Product Biosynthesis, NatPro