STRUCTURAL REFINEMENT OF THE NON-FLUORESCENT FLAVOPROTEIN FROM PHOTOBACTERIUM LEIOGNATHI AT 1.60 ANGSTROMS RESOLUTION

Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 A resolution.

Common Structural Features of the Luxf Protein and the Subunits of Bacterial Luciferase: Evidence for a (Beta(Slash)Alpha)8 Fold in Luciferase

Crystal Structure of a Flavoprotein Related to the Subunits of Bacterial Luciferase

Crystallization of Photobacterium Leiognathi Nfp, Non-Fluorescent Flavoprotein an Unusual Flavoprotein with Limited Sequence Identity to Bacterial Luciferase

MTKWNYGVFFLNFYHVGQQEPSLTMSNALETLRIIDEDTSIYDVVAFSEHHIDKSYNDETKLAPFVSLGKQIHVLATSPE
TVVKAAKYGMPLLFKWDDSQQKRIELLNHYQAAAAKFNVDIANVRHRLMLFVNVNDNPTQAKAELSIYLEDYLSYTQAET
SIDEIINSNAAGNFDTCLHHVAEMAQGLNNKVDFLFCFESMKDQENKKSLMINFDKRVINYRKEHNLN

THE STRUCTURAL FORMULA HYDROGEN ATOMS EQUIVALENTS PERTAIN TO THE OXIDIZED STATE OF FMN. THE CARBOXYLATE OF THE FATTY ACID IS IONIZED; IN ADDITION THE RIBOSE PHOSPHATE IS LIKELY SINGLY PROTONATED. THE PH OF THE CRYSTALS IS 5.5. THIS GIVES 43 HYDROGEN ATOMS FOR THE STRUCTURE, 8 ON THE ISOALLOXAZINE, 11 ON THE RIBOSE PHOSPHATE, AND 24 ON THE MYRISTATE. THE C3 OF THE FATTY ACID IS COVALENTLY LINKED TO C6 OF THE ISOALLOXAZINE NUCLEUS.

SYMMETRY
THE CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS PRESENTED
BELOW GENERATE THE SUBUNITS OF THE POLYMERIC MOLECULE.

APPLIED TO RESIDUES: 1 1 .. 423

TWO-FOLD AXIS AT 0,Y,1/4: THE MOLECULE IS A SYMMETRICAL
HOMODIMER.
SYMMETRY1 1 -1.000000 0.000000 0.000000 0.00000
SYMMETRY2 1 0.000000 1.000000 0.000000 0.00000
SYMMETRY3 1 0.000000 0.000000 -1.000000 49.66500

FLAVIN MONONUCLEOTIDE, MYRISTATE, FLAVOPROTEIN

MTKWNYGVFFLNFYHVGQQEPSLTMSNALETLRIIDEDTSIYDVVAFSEHHIDKSYNDETKLAPFVSLGKQIHILATSPE
TVVKAAKYGMPLLFKWDDSQQKRIELLNHYQAAAAKFNVDIAGVRHRLMLFVNVNDNPTQAKAELSIYLEDYLSYTQAET
SIDEIINSNAAGNFDTCLHHVAEMAQGLNNKVDFLFCFESMKDQENKKSLMINFDKRVINYRKEHNLN