STRUCTURE OF THE COMPLEX BETWEEN TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE AND N-HYDROXY-4-PHOSPHONO-BUTANAMIDE: BINDING AT THE ACTIVE SITE DESPITE AN "OPEN" FLEXIBLE LOOP

Structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: binding at the active site despite an "open" flexible loop conformation.

The Crystal Structure of the "Open" and the "Closed" Conformation of the Flexible Loop of Trypanosomal Triosephosphate Isomerase

Structure Determination of the Glycosomal Triosephosphate Isomerase from Trypanosoma Brucei Brucei at 2.4 Angstroms Resolution

Preliminary Crystallographic Studies of Triosephosphate Isomerase from the Blood Parasite Trypanosoma Brucei Brucei

MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSL
PILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWA
KVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGADVRGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKP
EFVDIIKATQ

SHEET
THE SHEETS PRESENTED AS *A* AND *B* ON SHEET RECORDS BELOW
ARE ACTUALLY EIGHT-STRANDED BETA-BARRELS. THESE ARE
REPRESENTED BY NINE-STRANDED SHEETS IN WHICH THE FIRST AND
LAST STRANDS ARE IDENTICAL.

SECONDARY STRUCTURE SPECIFICATIONS WERE MADE BY USE OF PROGRAM *DSSP* OF W. KABSCH AND C. SANDER.

THE ASYMMETRIC UNIT CONSISTS OF A DIMER. THE TWO MOLECULES HAVE BEEN ASSIGNED CHAIN INDICATORS *A* AND *B*. THE CRYSTALS USED FOR THIS STRUCTURE DETERMINATION WERE GROWN IN THE PRESENCE OF 2.4M AMMONIUM SULFATE (SEE PROTEIN DATA BANK ENTRY 2TIM), BUT BEFORE DATA COLLECTION THESE CRYSTALS WERE TRANSFERRED TO A MOTHER LIQUOR WITHOUT SULFATE. THE ACTIVE SITE OF SUBUNIT *A* CONTAINS THE INHIBITOR N-HYDROXY-4-PHOSPHONO-BUTANAMIDE (KI = 0.3 * 10**-3 M). IN THIS ENTRY THE FLEXIBLE LOOP (LOOP 6) OF EACH SUBUNIT IS IN AN OPEN CONFORMATION.

ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)