Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS 2 and DEBS 3: The A domain
The structure of docking domains in modular polyketide synthases.
ORF 2, 6-deoxyerythronolide B synthase II, DEBS 2
Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS 2 and DEBS 3: the B domain
The structure was determined using triple-resonance NMR spectroscopy. Intermolecular contacts were obtained from an X-filtered NOESY experiment on a mixed-labeled sample.
the structures are based on a total of 1811 restraints: 1709 NOE-derived distance constraints, 60 dihedral angle restraints, 42 distance restraints from hydrogen bonds.
1mM DOCK23 U-15N,13C: 100mM phosphate buffer NA: trace amounts of sodium azide, AEBSF protease inhibitor cocktail and TSP 1H shift reference: 90% H2O, 10% D2O
1mM DOCK23 (50% U-15N,13C: 50% unlabeled): 100mM phosphate buffer NA: trace amounts of sodium azide, AEBSF protease inhibitor cocktail and TSP 1H shift reference: 90% H2O, 10% D2O
FOUR HELIX BUNDLE, HOMODIMER, TRANSFERASE