CRYSTALLOGRAPHIC STRUCTURE OF GM23, MUTANT G89D, AN EXAMPLE OF CATALYTIC MIGRATION FROM TIM TO THIAMIN PHOSPHATE SYNTHASE.

Evolutionary Walk between (Beta/Alpha)(8) Barrels: Catalytic Migration from Triosephosphate Isomerase to Thiamin Phosphate Synthase.

DOUBLE CRYSTAL CHANNEL CUT, SI(111), 1M LONG RH COATED TOROIDAL MIRROR FOR VERTICAL AND HORIZONTAL FOCUSING.

PROTEIN WAS CRYSTALLIZED FROM 2M LI2SO4, 100 MM MES, PH 6.5

CRYSTALLOGRAPHIC BINDING STUDIES WITH AN ENGINEERED MONOMERIC VARIANT OF TRIOSEPHOSPHATE ISOMERASE

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

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

STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATEISOMERASE COMPLEXED WITH 3-PHOSPHOGLYCERATE

TRIOSEPHOSPHATE ISOMERASE COMPLEX WITH GLYCEROL-3- PHOSPHATE

CRYSTALLOGRAPHIC STRUCTURE OF GM23 AN EXAMPLE OF CATALYTIC MIGRATION FROM TIM TO THIAMIN PHOSPHATE SYNTHASE.

STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATEISOMERASE COMPLEXED WITH 3-PHOSPHONOPROPIONATE

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

STRUCTURE-BASED ENZYME ENGINEERING EFFORTS WITH AN INACTIVE MONOMERIC TIM VARIANT: THE IMPORTANCE OF A SINGLE POINT MUTATION FOR GENERATING AN ACTIVE SITE WITH SUITABLE BINDING PROPERTIES

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

STRUCTURES OF THE OPEN AND CLOSED STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE: AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM

TRIOSEPHOSPHATE ISOMERASE COMPLEX WITH 2-PHOSPHOGLYCERATE

TRIOSEPHOSPHATE ISOMERASE COMPLEX WITH SULFATE

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

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)

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

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

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

MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE

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

SHEET
DETERMINATION METHOD: DSSP
THE SHEETS PRESENTED AS "AA" 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 "BA" 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 "CA" 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 "DA" 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.

ENGINEERED RESIDUE IN CHAIN A, SER 43 TO PRO ENGINEERED RESIDUE IN CHAIN A, THR 44 TO SER ENGINEERED RESIDUE IN CHAIN A, PHE 45 TO TRP ENGINEERED RESIDUE IN CHAIN A, VAL 46 TO TYR ENGINEERED RESIDUE IN CHAIN A, HIS 47 TO MET ENGINEERED RESIDUE IN CHAIN A, LEU 48 TO GLN ENGINEERED RESIDUE IN CHAIN A, ILE 68 TO GLY ENGINEERED RESIDUE IN CHAIN A, ALA 69 TO ASN ENGINEERED RESIDUE IN CHAIN A, LYS 70 TO ALA ENGINEERED RESIDUE IN CHAIN A, SER 71 TO ASP ENGINEERED RESIDUE IN CHAIN A, SER 79 TO ALA ENGINEERED RESIDUE IN CHAIN A, PRO 81 TO ALA ENGINEERED RESIDUE IN CHAIN A, ILE 82 TO SER ENGINEERED RESIDUE IN CHAIN A, VAL 88 TO ILE ENGINEERED RESIDUE IN CHAIN A, ASN 89 TO SER ENGINEERED RESIDUE IN CHAIN A, GLY 94 TO ASP ENGINEERED RESIDUE IN CHAIN A, GLU 135 TO SER ENGINEERED RESIDUE IN CHAIN A, ALA 148 TO THR ENGINEERED RESIDUE IN CHAIN A, ILE 198 TO VAL ENGINEERED RESIDUE IN CHAIN A, LYS 217 TO ARG ENGINEERED RESIDUE IN CHAIN A, GLN 250 TO GLU ENGINEERED RESIDUE IN CHAIN B, SER 43 TO PRO ENGINEERED RESIDUE IN CHAIN B, THR 44 TO SER ENGINEERED RESIDUE IN CHAIN B, PHE 45 TO TRP ENGINEERED RESIDUE IN CHAIN B, VAL 46 TO TYR ENGINEERED RESIDUE IN CHAIN B, HIS 47 TO MET ENGINEERED RESIDUE IN CHAIN B, LEU 48 TO GLN ENGINEERED RESIDUE IN CHAIN B, ILE 68 TO GLY ENGINEERED RESIDUE IN CHAIN B, ALA 69 TO ASN ENGINEERED RESIDUE IN CHAIN B, LYS 70 TO ALA ENGINEERED RESIDUE IN CHAIN B, SER 71 TO ASP ENGINEERED RESIDUE IN CHAIN B, SER 79 TO ALA ENGINEERED RESIDUE IN CHAIN B, PRO 81 TO ALA ENGINEERED RESIDUE IN CHAIN B, ILE 82 TO SER ENGINEERED RESIDUE IN CHAIN B, VAL 88 TO ILE ENGINEERED RESIDUE IN CHAIN B, ASN 89 TO SER ENGINEERED RESIDUE IN CHAIN B, GLY 94 TO ASP ENGINEERED RESIDUE IN CHAIN B, GLU 135 TO SER ENGINEERED RESIDUE IN CHAIN B, ALA 148 TO THR ENGINEERED RESIDUE IN CHAIN B, ILE 198 TO VAL ENGINEERED RESIDUE IN CHAIN B, LYS 217 TO ARG ENGINEERED RESIDUE IN CHAIN B, GLN 250 TO GLU ENGINEERED RESIDUE IN CHAIN C, SER 43 TO PRO ENGINEERED RESIDUE IN CHAIN C, THR 44 TO SER ENGINEERED RESIDUE IN CHAIN C, PHE 45 TO TRP ENGINEERED RESIDUE IN CHAIN C, VAL 46 TO TYR ENGINEERED RESIDUE IN CHAIN C, HIS 47 TO MET ENGINEERED RESIDUE IN CHAIN C, LEU 48 TO GLN ENGINEERED RESIDUE IN CHAIN C, ILE 68 TO GLY ENGINEERED RESIDUE IN CHAIN C, ALA 69 TO ASN ENGINEERED RESIDUE IN CHAIN C, LYS 70 TO ALA ENGINEERED RESIDUE IN CHAIN C, SER 71 TO ASP ENGINEERED RESIDUE IN CHAIN C, SER 79 TO ALA ENGINEERED RESIDUE IN CHAIN C, PRO 81 TO ALA ENGINEERED RESIDUE IN CHAIN C, ILE 82 TO SER ENGINEERED RESIDUE IN CHAIN C, VAL 88 TO ILE ENGINEERED RESIDUE IN CHAIN C, ASN 89 TO SER ENGINEERED RESIDUE IN CHAIN C, GLY 94 TO ASP ENGINEERED RESIDUE IN CHAIN C, GLU 135 TO SER ENGINEERED RESIDUE IN CHAIN C, ALA 148 TO THR ENGINEERED RESIDUE IN CHAIN C, ILE 198 TO VAL ENGINEERED RESIDUE IN CHAIN C, LYS 217 TO ARG ENGINEERED RESIDUE IN CHAIN C, GLN 250 TO GLU ENGINEERED RESIDUE IN CHAIN D, SER 43 TO PRO ENGINEERED RESIDUE IN CHAIN D, THR 44 TO SER ENGINEERED RESIDUE IN CHAIN D, PHE 45 TO TRP ENGINEERED RESIDUE IN CHAIN D, VAL 46 TO TYR ENGINEERED RESIDUE IN CHAIN D, HIS 47 TO MET ENGINEERED RESIDUE IN CHAIN D, LEU 48 TO GLN ENGINEERED RESIDUE IN CHAIN D, ILE 68 TO GLY ENGINEERED RESIDUE IN CHAIN D, ALA 69 TO ASN ENGINEERED RESIDUE IN CHAIN D, LYS 70 TO ALA ENGINEERED RESIDUE IN CHAIN D, SER 71 TO ASP ENGINEERED RESIDUE IN CHAIN D, SER 79 TO ALA ENGINEERED RESIDUE IN CHAIN D, PRO 81 TO ALA ENGINEERED RESIDUE IN CHAIN D, ILE 82 TO SER ENGINEERED RESIDUE IN CHAIN D, VAL 88 TO ILE ENGINEERED RESIDUE IN CHAIN D, ASN 89 TO SER ENGINEERED RESIDUE IN CHAIN D, GLY 94 TO ASP ENGINEERED RESIDUE IN CHAIN D, GLU 135 TO SER ENGINEERED RESIDUE IN CHAIN D, ALA 148 TO THR ENGINEERED RESIDUE IN CHAIN D, ILE 198 TO VAL ENGINEERED RESIDUE IN CHAIN D, LYS 217 TO ARG ENGINEERED RESIDUE IN CHAIN D, GLN 250 TO GLU
THE SEQUENCE DEPOSITED IN THIS ENTRY IS 87.9 PER CENT IDENTICAL TO UNIPROT P04789

TRIOSE-PHOSPHATE ISOMERASE (E.C.5.3.1.1)

CHAIN A AND (RESSEQ 22:35 OR RESSEQ 37:68 OR RESSEQ 70:265 )

CHAIN B AND (RESSEQ 22:35 OR RESSEQ 37:68 OR RESSEQ 70:265 )

CHAIN C AND (RESSEQ 22:35 OR RESSEQ 37:68 OR RESSEQ 70:265 )

CHAIN D AND (RESSEQ 22:35 OR RESSEQ 37:68 OR RESSEQ 70:265 )