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1TPF
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COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS
Descriptor: DIMETHYL SULFOXIDE, TRIOSEPHOSPHATE ISOMERASE
Authors:Radha Kishan, K.V, Zeelen, J.Ph, Wierenga, R.K.
Deposit date:1994-02-28
Release date:1994-05-31
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms.
Protein Sci., 3, 1994
1TTI
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THREE NEW CRYSTAL STRUCTURES OF POINT MUTATION VARIANTS OF MONOTIM: CONFORMATIONAL FLEXIBILITY OF LOOP-1,LOOP-4 AND LOOP-8
Descriptor: 2-PHOSPHOGLYCOLIC ACID, TRIOSEPHOSPHATE ISOMERASE
Authors:Radha Kishan, K.V, Wierenga, R.K.
Deposit date:1995-04-19
Release date:1995-10-15
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8.
Structure, 3, 1995
1TRI
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THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP
Descriptor: SULFATE ION, TRIOSEPHOSPHATE ISOMERASE
Authors:Wierenga, R.K.
Deposit date:1993-10-08
Release date:1994-07-31
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:The crystal structure of an engineered monomeric triosephosphate isomerase, monoTIM: the correct modelling of an eight-residue loop.
Structure, 1, 1993
1TPV
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S96P CHANGE IS A SECOND-SITE SUPPRESSOR FOR H95N SLUGGISH MUTANT TRIOSEPHOSPHATE ISOMERASE
Descriptor: PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE
Authors:Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Stock, A.M, Narayana, N, Xuong, Ng.H, Knowles, J.R, Petsko, G.A, Ringe, D.
Deposit date:1994-11-07
Release date:1995-04-20
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:The structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase.
Biochemistry, 35, 1996
1TPH
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1.8 ANGSTROMS CRYSTAL STRUCTURE OF WILD TYPE CHICKEN TRIOSEPHOSPHATE ISOMERASE-PHOSPHOGLYCOLOHYDROXAMATE COMPLEX
Descriptor: PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE
Authors:Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Knowles, J.R, Petsko, G.A, Ringe, D.
Deposit date:1993-12-22
Release date:1994-04-30
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution.
Biochemistry, 33, 1994
1TPW
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TRIOSEPHOSPHATE ISOMERASE DRINKS WATER TO KEEP HEALTHY
Descriptor: PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE
Authors:Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Stock, A.M, Narayana, N, Xuong, Ng.H, Knowles, J.R, Petsko, G.A, Ringe, D.
Deposit date:1994-11-07
Release date:1995-04-20
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:The role of water in the catalytic efficiency of triosephosphate isomerase.
Biochemistry, 38, 1999
1TSI
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STRUCTURE OF THE COMPLEX BETWEEN TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE AND N-HYDROXY-4-PHOSPHONO-BUTANAMIDE: BINDING AT THE ACTIVE SITE DESPITE AN "OPEN" FLEXIBLE LOOP
Descriptor: N-HYDROXY-4-PHOSPHONO-BUTANAMIDE, TRIOSEPHOSPHATE ISOMERASE
Authors:Verlinde, C.L.M.J.
Deposit date:1992-11-19
Release date:1994-01-31
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.84 Å)
Cite: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.
Protein Sci., 1, 1992
1TPC
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OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE
Descriptor: PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE
Authors:Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Knowles, J.R, Petsko, G.A, Ringe, D.
Deposit date:1994-02-03
Release date:1995-02-14
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules.
Biochemistry, 34, 1995
1TPU
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S96P CHANGE IS A SECOND-SITE SUPPRESSOR FOR H95N SLUGGISH MUTANT TRIOSEPHOSPHATE ISOMERASE
Descriptor: PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE
Authors:Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Stock, A.M, Narayana, N, Xuong, Ng.H, Knowles, J.R, Petsko, G.A, Ringe, D.
Deposit date:1994-11-07
Release date:1995-04-20
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:The structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase.
Biochemistry, 35, 1996
1W0M
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Triosephosphate isomerase from Thermoproteus tenax
Descriptor: PHOSPHATE ION, TRIOSEPHOSPHATE ISOMERASE
Authors:Walden, H, Taylor, G, Lorentzen, E, Pohl, E, Lilie, H, Schramm, A, Knura, T, Stubbe, K, Tjaden, B, Hensel, R.
Deposit date:2004-06-08
Release date:2004-09-09
Last modified:2019-07-24
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Structure and Function of a Regulated Archaeal Triosephosphate Isomerase Adapted to High Temperature
J.Mol.Biol., 342, 2004
1VGA
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Structures of unligated and inhibitor complexes of W168F mutant of Triosephosphate Isomerase from Plasmodium falciparum
Descriptor: Triosephosphate isomerase
Authors:Eaazhisai, K, Balaram, H, Balaram, P, Murthy, M.R.N.
Deposit date:2004-04-23
Release date:2004-10-26
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structures of Unliganded and Inhibitor Complexes of W168F, a Loop6 Hinge Mutant of Plasmodium falciparum Triosephosphate Isomerase: Observation of an Intermediate Position of Loop6
J.Mol.Biol., 343, 2004
1WOB
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Structure of a loop6 hinge mutant of Plasmodium falciparum Triosephosphate Isomerase, W168F, complexed to sulfate
Descriptor: SULFATE ION, Triosephosphate isomerase
Authors:Eaazhisai, K, Balaram, H, Balaram, P, Murthy, M.R.N.
Deposit date:2004-08-12
Release date:2004-10-26
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:Structures of Unliganded and Inhibitor Complexes of W168F, a Loop6 Hinge Mutant of Plasmodium falciparum Triosephosphate Isomerase: Observation of an Intermediate Position of Loop6
J.Mol.Biol., 343, 2004
1WOA
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Structure of the loop6 hinge mutant of Plasmodium falciparum Triosephosphate Isomerase, W168F, complexed with Glycerol-2-phosphate
Descriptor: 2-HYDROXY-1-(HYDROXYMETHYL)ETHYL DIHYDROGEN PHOSPHATE, Triosephosphate isomerase
Authors:Eaazhisai, K, Balaram, H, Balaram, P, Murthy, M.R.N.
Deposit date:2004-08-12
Release date:2004-10-26
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:Structures of Unliganded and Inhibitor Complexes of W168F, a Loop6 Hinge Mutant of Plasmodium falciparum Triosephosphate Isomerase: Observation of an Intermediate Position of Loop6
J.Mol.Biol., 343, 2004
1WYI
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human triosephosphate isomerase of new crystal form
Descriptor: Triosephosphate isomerase
Authors:Kinoshita, T.
Deposit date:2005-02-14
Release date:2005-04-12
Last modified:2024-03-13
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method.
Acta Crystallogr.,Sect.F, 61, 2005
2VFH
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Crystal structure of the F96W mutant of Plasmodium falciparum triosephosphate isomerase complexed with 3-phosphoglycerate
Descriptor: 3-PHOSPHOGLYCERIC ACID, TRIOSEPHOSPHATE ISOMERASE
Authors:Gayathri, P, Banerjee, M, Vijayalakshmi, A, Balaram, H, Balaram, P, Murthy, M.R.N.
Deposit date:2007-11-04
Release date:2008-12-09
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2 Å)
Cite:Biochemical and Structural Characterization of Residue 96 Mutants of Plasmodium Falciparum Triosephosphate Isomerase: Active-Site Loop Conformation, Hydration and Identification of a Dimer-Interface Ligand-Binding Site.
Acta Crystallogr.,Sect.D, 65, 2009
2VFI
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Crystal structure of the Plasmodium falciparum triosephosphate isomerase in the loop closed state with 3-phosphoglycerate bound at the active site and interface
Descriptor: 3-PHOSPHOGLYCERIC ACID, TRIOSEPHOSPHATE ISOMERASE
Authors:Gayathri, P, Banerjee, M, Vijayalakshmi, A, Balaram, H, Balaram, P, Murthy, M.R.N.
Deposit date:2007-11-04
Release date:2008-12-09
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2.25 Å)
Cite:Biochemical and Structural Characterization of Residue 96 Mutants of Plasmodium Falciparum Triosephosphate Isomerase: Active-Site Loop Conformation, Hydration and Identification of a Dimer-Interface Ligand-Binding Site.
Acta Crystallogr.,Sect.D, 65, 2009
2VEN
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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
Descriptor: CITRIC ACID, GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE
Authors:Alahuhta, M, Salin, M, Casteleijn, M.G, Kemmer, C, El-Sayed, I, Augustyns, K, Neubauer, P, Wierenga, R.K.
Deposit date:2007-10-25
Release date:2008-02-19
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2 Å)
Cite:Structure-Based Protein Engineering Efforts with a Monomeric Tim Variant: The Importance of a Single Point Mutation for Generating an Active Site with Suitable Binding Properties.
Protein Eng.Des.Sel., 21, 2008
2V0T
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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
Descriptor: 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL
Authors:Alahuhta, M, Casteleijn, M.G, Neubauer, P, Wierenga, R.K.
Deposit date:2007-05-18
Release date:2008-02-19
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2.2 Å)
Cite: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.
Acta Crystallogr. D Biol. Crystallogr., 64, 2008
2V5L
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Structures of the Open and Closed State of Trypanosomal Triosephosphate Isomerase: as Observed in a New Crystal Form: Implications for the Reaction Mechanism
Descriptor: SULFATE ION, TRIOSEPHOSPHATE ISOMERASE
Authors:Noble, M.E.M, Zeelen, J.P, Wierenga, R.K.
Deposit date:2007-07-06
Release date:2007-07-31
Last modified:2018-04-04
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:Structures of the Open and Closed State of Trypanosomal Triosephosphate Isomerase: As Observed in a New Crystal Form: Implications for the Reaction Mechanism
Proteins: Struct.,Funct., Genet., 16, 1993
2VFE
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Crystal structure of F96S mutant of Plasmodium falciparum triosephosphate isomerase with 3- phosphoglycerate bound at the dimer interface
Descriptor: 3-PHOSPHOGLYCERIC ACID, GLYCEROL, TRIOSEPHOSPHATE ISOMERASE
Authors:Gayathri, P, Banerjee, M, Vijayalakshmi, A, Balaram, H, Balaram, P, Murthy, M.R.N.
Deposit date:2007-11-03
Release date:2008-12-09
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Biochemical and Structural Characterization of Residue 96 Mutants of Plasmodium Falciparum Triosephosphate Isomerase: Active-Site Loop Conformation, Hydration and Identification of a Dimer-Interface Ligand-Binding Site.
Acta Crystallogr.,Sect.D, 65, 2009
2VEI
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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
Descriptor: GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE, SULFATE ION
Authors:Alahuhta, M, Salin, M, Casteleijn, M.G, Kemmer, C, El-Sayed, I, Augustyns, K, Neubauer, P, Wierenga, R.K.
Deposit date:2007-10-24
Release date:2008-02-19
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (1.89 Å)
Cite:Structure-Based Protein Engineering Efforts with a Monomeric Tim Variant: The Importance of a Single Point Mutation for Generating an Active Site with Suitable Binding Properties.
Protein Eng.Des.Sel., 21, 2008
2V2C
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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
Descriptor: 2-PHOSPHOGLYCOLIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL
Authors:Alahuhta, M, Casteleijn, M.G, Neubauer, P, Wierenga, R.K.
Deposit date:2007-06-05
Release date:2008-02-19
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (1.89 Å)
Cite: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.
Acta Crystallogr.,Sect.D, 64, 2008
2VEM
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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
Descriptor: (3-bromo-2-oxo-propoxy)phosphonic acid, GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE, TERTIARY-BUTYL ALCOHOL
Authors:Alahuhta, M, Salin, M, Casteleijn, M.G, Kemmer, C, El-Sayed, I, Augustyns, K, Neubauer, P, Wierenga, R.K.
Deposit date:2007-10-25
Release date:2008-02-19
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Structure-Based Protein Engineering Efforts with a Monomeric Tim Variant: The Importance of a Single Point Mutation for Generating an Active Site with Suitable Binding Properties.
Protein Eng.Des.Sel., 21, 2008
2V5B
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The monomerization of Triosephosphate Isomerase from Trypanosoma cruzi
Descriptor: TRIOSEPHOSPHATE ISOMERASE
Authors:Arreola, R, Torres-Larios, A.
Deposit date:2008-10-02
Release date:2008-11-11
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2 Å)
Cite:The Monomerization of Triosephosphate Isomerase from Trypanosoma Cruzi.
Prog.Nucleic Acid Res. Mol.Biol., 84, 2008
2VFF
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Crystal structure of the F96H mutant of Plasmodium falciparum triosephosphate isomerase
Descriptor: TRIOSEPHOSPHATE ISOMERASE
Authors:Gayathri, P, Banerjee, M, Vijayalakshmi, A, Balaram, H, Balaram, P, Murthy, M.R.N.
Deposit date:2007-11-04
Release date:2008-12-09
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Biochemical and Structural Characterization of Residue 96 Mutants of Plasmodium Falciparum Triosephosphate Isomerase: Active-Site Loop Conformation, Hydration and Identification of a Dimer-Interface Ligand-Binding Site.
Acta Crystallogr.,Sect.D, 65, 2009

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