CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH INDOLE PROPANOL PHOSPHATE

Crystal Structure of Wild-Type Tryptophan Synthase Complexed with the Natural Substrate Indole-3-Glycerol Phosphate

INHIBITOR INDOLE PROPANOL PHOSPHATE BOUND TO THE ALPHA SITE

ENZYME SOLUTION: 10 MG/ML TRPS IN 50 MM BICINE PH 7.8, 1 MM EDTA, 5 MM DITHIOERYTHRITOL, 20 MUM PYRIDOXAL-5'-PHOSPHATE. RESERVOIR SOLUTION: 50 MM BICINE PH 7.8, 5 MM EDTA, 5 MM DITHIOERYTHRITOL, 0.1 MM PYRIDOXAL-5'-PHOSPHATE, 2 MM SPERMINE, 8-12 % PEG 8000. HANGING DROP GEOMETRY, CRYSTALLIZATION DROP CONSISTED AN INITIAL INDOLE PROPANOLE PHOSPHATE (IPL) CONCENTRATION OF 7 MM

CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE

TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) IN THE PRESENCE OF CESIUM, ROOM TEMPERATURE

TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) IN THE PRESENCE OF POTASSIUM AT ROOM TEMPERATURE

CRYSTAL STRUCTURES OF MUTANT (BETAK87T) TRYPTOPHAN SYNTHASE ALPHA-2 BETA-2 COMPLEX WITH LIGANDS BOUND TO THE ACTIVE SITES OF THE ALPHA AND BETA SUBUNITS REVEAL LIGAND-INDUCED CONFORMATIONAL CHANGES

TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) WITH A MUTATION OF LYS 87 ->THR IN THE B SUBUNIT AND IN THE PRESENCE OF LIGAND L-SERINE

CRYO-CRYSTALLOGRAPHY OF A TRUE SUBSTRATE, INDOLE-3-GLYCEROL PHOSPHATE, BOUND TO A MUTANT (ALPHAD60N) TRYPTOPHAN SYNTHASE ALPHA2BETA2 COMPLEX REVEALS THE CORRECT ORIENTATION OF ACTIVE SITE ALPHA GLU 49

CRYO-CRYSTALLOGRAPHY OF A TRUE SUBSTRATE, INDOLE-3-GLYCEROL PHOSPHATE, BOUND TO A MUTANT (ALPHAD60N) TRYPTOPHAN SYNTHASE (ALPHA)2(BETA)2 COMPLEX REVEALS THE CORRECT ORIENTATION OF ACTIVE SITE ALPHA GLU 49

CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUOROINDOLE PROPANOL PHOSPHATE AND L-SER BOUND AS AMINO ACRYLATE TO THE BETA SITE

CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUOROINDOLE PROPANOL PHOSPHATE

TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) FROM SALMONELLA TYPHIMURIUM

CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH INDOLE GLYCEROL PHOSPHATE

HELIX
DETERMINATION METHOD: DSSP, KABSCH & SANDER

SHEET
DETERMINATION METHOD: DSSP, KABSCH & SANDER

RESIDUES A156, A157 AND A158 WERE MODELED IN TWO CONFORMATIONS INCLUDING THE MAIN CHAIN ATOMS. THE SIDE CHAINS OF RESIDUES ILE A30, GLU A31, CYS A154, SER A178 AND GLU A254 WERE MODELED IN TWO CONFORMATIONS THE SIDE CHAINS OF RESIDUES GLU B11, MET B22, LYS B37, LYS B50, LYS B61, ILE B65, MET B152, THR B165, LYS B219, MET B240, HIS B260, ARG B341, GLU B367 AND ARG B379 WERE MODELED IN TWO CONFORMATIONS

TRYPTOPHAN SYNTHASE ALPHA CHAIN (E.C.4.2.1.20), TRYPTOPHAN SYNTHASE BETA CHAIN (E.C.4.2.1.20)

BIOMOLECULE THE BIOLOGICALLY ACTIVE MOLECULE IS ATETRAMER OF TWO ALPHA AND TWO BETA CHAINS.

LYASE, CARBON-OXYGEN LYASE, TRYPTOPHAN BIOSYNTHESIS, PYRIDOXAL PHOSPHATE