X-ray crystal structure of 5'-fluorodeoxyadenosine synthase s158g mutant complexed with 5'-fluorodeoxyadenosin

Mechanism of enzymatic fluorination in Streptomyces cattleya.

0.1M CITRATE-PHOSPHATE BUFFER PH4.6, 20%PEG1000, 0.2M LI2SO4

CRYSTAL STRUCTURE AND MECHANISM OF A BACTERIAL FLUORINATINGENZYME, PRODUCT COMPLEX

X-RAY CRYSTAL STRUCTURE OF 5'- FLUORODEOXYADENOSINE SYNTHASE FROM STREPTOMYCES CATTLEYA COMPLEXED WITH AN INHIBITOR, AN ANALOGUE OF S-ADENOSYL METHIONINE

X-RAY CRYSTAL STRUCTUE OF 5'- FLUORODEOXYADENOSINE SYNTHASE FROM STREPTOMYCES CATTLEYA COMPLEXED WITH 2'DEOXY-5'DEOXY- FLUOROADENOSINE.

X-RAY CRYSTAL STRUCTURE OF 5- FLUORODEOXYADENOSINE SYNTHASE FROM STREPTOMYCES CATTLEYA COMPLEXED WITH 5-DEOXY-ADENOSINE

CRYSTAL STRUCTURE AND MECHANISM OF A BACTERIAL FLUORINATINGENZYME

THE FLUORINASE FROM STREPTOMYCES CATTLEYA IS ALSO A CHLORINASE. STRUCTURE OF 5'-CHLORO- 5'-DEOXYADENOSINE CRSTALLISED IN THE FLUORINASE.

CRYSTAL STRUCTURE OF THE APO FORM OF THE 5'-FLUORO-5'-DEOXYADENOSINE SYNTHASE ENZYME FROM STREPTOMYCES CATTLEYA

X-RAY CRYSTAL STRUCTURE OF 5'- FLUORODEOXYADENOSINE SYNTHASE FROM STREPTOMYCES CATTLEYA COMPLEXED WITH BETA-D- ERYTHROFURANOSYL-ADENOSINE

X-RAY CRYSTAL STRUCTURE OF 5'- FLUORODEOXYADENOSINE SYNTHASE FROM STREPTOMYCES CATTLEYA COMPLEXED WITH 5'DEOXYADENOSINE

THE STRUCTURAL BASIS OF THE MECHANISM OF THE FLUORINASE IN STREPTOMYCES CATTLEYA

X-RAY CRYSTAL STRUCTURE OF 5'- FLUORODEOXYADENOSINE SYNTHASE FROM STREPTOMYCES CATTLEYA COMPLEXED WITH 5'-FLUORO-ADENOSINE

X-RAY CRYSTAL STRUCTURE OF 5'- FLUORODEOXYADENOSINE SYNTHASE S158A MUTANT FROM STREPTOMYCES CATTLEYA COMPLEXED WITH THE PRODUCTS, FDA AND MET

SHEET
DETERMINATION METHOD: DSSP
THE SHEETS PRESENTED AS "AB", "BB" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

THE SHEETS PRESENTED AS "CB" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY
A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

ENGINEERED RESIDUE IN CHAIN A, SER 158 TO GLY ENGINEERED RESIDUE IN CHAIN B, SER 158 TO GLY ENGINEERED RESIDUE IN CHAIN C, SER 158 TO GLY

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

FLUORINATION, TRANSFERASE, BIOSYNTHETIC PROTEIN