The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM

Structural Studies Show that the A178L Mutation in the C-Terminal Hinge of the Catalytic Loop-6 of Triosephosphate Isomerase (Tim) Induces a Closed- Like Conformation in Dimeric and Monomeric Tim.

FLAT PRE-MIRROR AND BENT, VERTICALLY FOCUSSING

MSKPQPIAAANWKSGSPDSLSELIDLFNSTSINHDVQCVVASTFVHLAMTKERLSHPKFVIAAQNAGNADALASLKDFGV
NWIVLGHSERRWYYGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEP
VWAIGTGKVLTPQQAQEAHALIRSWVSSKIGADVAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKA
TQ

MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE

CRYSTAL STRUCTURE OF TRIOSE-PHOSPHATE ISOMERASE WITH MODIFIED SUBSTRATE BINDING SITE

STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATEISOMERASE COMPLEXED WITH 3- PHOSPHONOPROPIONATE

STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATEISOMERASE COMPLEXED WITH 3- PHOSPHOGLYCERATE

STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TIM WITH THE SALT-BRIDGE-FORMING RESIDUE ARG191 MUTATED TO SER

PROTEIN ENGINEERING WITH MONOMERIC TRIOSEPHOSPHATEISOMERASE: THE MODELLING AND STRUCTURE VERIFICATION OFA SEVEN RESIDUE LOOP

TRIOSEPHOSPHATE ISOMERASE MUTANT WITH PHE 45 REPLACED BY SER, VAL 46 REPLACED BY SER, AND RESIDUES 68 - 82 REPLACED BY THE RESIDUES GNADALAS (F45S,V46S,68-82:GNADALAS )

TRIOSEPHOSPHATE ISOMERASE MUTANT WITH 15 RESIDUES (68 - 82) REPLACED BY 8 RESIDUES

TRIOSEPHOSPHATE ISOMERASE COMPLEX WITH N- HYDROXY-4-PHOSPHONO-BUTANAMIDE

MOL_ID: 1; MOLECULE: TRIOSEPHOSPHATE ISOMERASE ; CHAIN: NULL; EC: 5.3.1.1; ENGINEERED: YES; MUTATION: I68G, A69N, K70A, S71D, DEL( 73-79), P81A, A100W; OTHER_DETAILS: MONOTIM WITH A110W MUTATION

MOL_ID: 1; MOLECULE: TRIOSEPHOSPHATE ISOMERASE ; CHAIN: NULL; EC: 5.3.1.1; MUTATION: VARIANT OF MONOTIM WITH PHE 45 REPLACED BY SER AND VAL 46 REPLACED BY SER (F45S, V46S) AND 73 - 79 DELETED

THE FUNCTIONAL ROLE OF THE CONSERVED ACTIVE SITE PROLINE OF TRIOSEPHOSPHATE ISOMERASE

TRIOSEPHOSPHATE ISOMERASE COMPLEX WITH 2- PHOSPHOGLYCERATE

TRIOSEPHOSPHATE ISOMERASE COMPLEX WITH SULFATE

TRIOSEPHOSPHATE ISOMERASE COMPLEX WITH GLYCEROL -3-PHOSPHATE

SHEET
DETERMINATION METHOD: DSSP
THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY
A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

GLUCONEOGENESIS, LIPID SYNTHESIS, ENGINEERING, PENTOSE SHUNT, POINT MUTATION, TIM, A178L, LOOP6, HINGE, LOOP-6, ENZYME, ISOMERASE, FATTY ACID BIOSYNTHESIS, TRIOSEPHOSPHATE ISOMERASE, GLYCOSOME, MONOMERIC, TIM-BARREL, GLYCOLYSIS