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PDB: 51 results

2J27
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The functional role of the conserved active site proline of triosephosphate isomerase.
Descriptor: 2-PHOSPHOGLYCOLIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL
Authors:Casteleijn, M.G, Alahuhta, M, Groebel, K, El-Sayed, I, Augustyns, K, Lambeir, A.M, Neubauer, P, Wierenga, R.K.
Deposit date:2006-08-16
Release date:2007-01-02
Last modified:2024-05-01
Method:X-RAY DIFFRACTION (1.15 Å)
Cite:Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase.
Biochemistry, 45, 2006
2V2H
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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, CHLORIDE ION, TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL
Authors:Alahuhta, M, Casteleijn, M.G, Neubauer, P, Wierenga, R.K.
Deposit date:2007-06-06
Release date:2008-02-19
Last modified:2024-05-01
Method:X-RAY DIFFRACTION (1.18 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
4PC8
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Structure-based protein engineering efforts on the scaffold of a monomeric triosephosphate isomerase yielding a sugar isomerase
Descriptor: GLYCOLIC ACID, Ma21-TIM
Authors:Krause, M, Neubauer, P, Wierenga, R.K.
Deposit date:2014-04-14
Release date:2015-04-22
Last modified:2023-11-15
Method:X-RAY DIFFRACTION (1.55 Å)
Cite:Crystal structures of two monomeric triosephosphate isomerase variants identified via a directed-evolution protocol selecting for L-arabinose isomerase activity.
Acta Crystallogr.,Sect.F, 72, 2016
2VEK
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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-(BUTYLSULPHONYL)-PROPANOIC ACID, CITRIC ACID, 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:2007-10-24
Release date:2008-02-19
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (1.6 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
1KV5
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Structure of Trypanosoma brucei brucei TIM with the salt-bridge-forming residue Arg191 mutated to Ser
Descriptor: 2,3-DIHYDROXY-1,4-DITHIOBUTANE, 2-PHOSPHOGLYCOLIC ACID, GLYCEROL, ...
Authors:Kursula, I, Partanen, S, Lambeir, A.-M, Wierenga, R.K.
Deposit date:2002-01-25
Release date:2002-03-29
Last modified:2023-08-16
Method:X-RAY DIFFRACTION (1.65 Å)
Cite:The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis
FEBS Lett., 518, 2002
2WSR
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BU of 2wsr by Molmil
MONOTIM MUTANT RMM0-1, MONOMERIC FORM.
Descriptor: AZIDE ION, SULFATE ION, TRIOSE PHOSPHATE ISOMERASE, ...
Authors:Rudino-Pinera, E, Rojas-Trejo, S.P, Arreola, R, Saab-Rincon, G, Soberon, X, Horjales, E.
Deposit date:2009-09-08
Release date:2009-09-15
Last modified:2023-12-20
Method:X-RAY DIFFRACTION (1.65 Å)
Cite:Space Group Transition Driven by Temperature and Related to Monomer-Dimer Transition in Solution: The Case of Monomeric Tim of Trypanosoma Brucei Brucei
To be Published
3Q37
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Identification of Amino Acids that Account for Long-Range Interactions in Proteins Using Two Triosephosphate Isomerases from Pathogenic Trypanosomes.
Descriptor: TIM from Trypanosoma cruzi/ TIM from Trypanosoma brucei brucei chimera protein
Authors:Garcia-Torres, I, Cabrera, N, Torres-Larios, A, Rodriguez-Bolanos, M, Gomez-Puyou, A, Perez-Montfort, R.
Deposit date:2010-12-21
Release date:2011-09-14
Last modified:2023-09-13
Method:X-RAY DIFFRACTION (1.65 Å)
Cite:Identification of amino acids that account for long-range interactions in two triosephosphate isomerases from pathogenic trypanosomes.
Plos One, 6, 2011
5I3F
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Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase
Descriptor: Triosephosphate isomerase, glycosomal
Authors:Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J.
Deposit date:2016-02-10
Release date:2016-05-18
Last modified:2023-09-27
Method:X-RAY DIFFRACTION (1.72 Å)
Cite:Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
Biochemistry, 55, 2016
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
5I3J
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Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase
Descriptor: SODIUM ION, Triosephosphate isomerase, glycosomal
Authors:Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J.
Deposit date:2016-02-10
Release date:2016-05-18
Last modified:2023-09-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
Biochemistry, 55, 2016
2X1T
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Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase
Descriptor: 4-PHOSPHO-D-ERYTHRONOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL
Authors:Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Casteleijn, M.G, Neubauer, P, Salmon, L, Wierenga, R.
Deposit date:2010-01-04
Release date:2010-01-26
Last modified:2023-12-20
Method:X-RAY DIFFRACTION (1.83 Å)
Cite:Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase
Acta Crystallogr.,Sect.D, 66, 2010
5TIM
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BU of 5tim by Molmil
REFINED 1.83 ANGSTROMS STRUCTURE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, CRYSTALLIZED IN THE PRESENCE OF 2.4 M-AMMONIUM SULPHATE. A COMPARISON WITH THE STRUCTURE OF THE TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE-GLYCEROL-3-PHOSPHATE COMPLEX
Descriptor: 2,3-DIHYDROXY-1,4-DITHIOBUTANE, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE
Authors:Wierenga, R.K, Hol, W.G.J.
Deposit date:1991-04-23
Release date:1992-10-15
Last modified:2024-03-06
Method:X-RAY DIFFRACTION (1.83 Å)
Cite:Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex.
J.Mol.Biol., 220, 1991
2X1U
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Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase
Descriptor: SULFATE ION, TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL
Authors:Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Casteleijn, M.G, Neubauer, P, Salmon, L, Wierenga, R.
Deposit date:2010-01-04
Release date:2010-01-26
Last modified:2023-12-20
Method:X-RAY DIFFRACTION (1.84 Å)
Cite:Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase
Acta Crystallogr.,Sect.D, 66, 2010
2V2C
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BU of 2v2c by Molmil
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:2024-05-01
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
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
2X2G
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BU of 2x2g by Molmil
CRYSTALLOGRAPHIC BINDING STUDIES WITH AN ENGINEERED MONOMERIC VARIANT OF TRIOSEPHOSPHATE ISOMERASE
Descriptor: 3-PHOSPHOGLYCERIC ACID, TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL
Authors:Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Casteleijn, M.G, Neubauer, P, Salmon, L, Wierenga, R.
Deposit date:2010-01-13
Release date:2010-01-26
Last modified:2023-12-20
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase
Acta Crystallogr.,Sect.D, 66, 2010
2X1S
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Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase
Descriptor: 3-SULFOPROPANOIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE, ...
Authors:Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Castejeijn, M.G, Neubauer, P, Salmon, L, Wierenga, R.
Deposit date:2010-01-04
Release date:2010-01-26
Last modified:2023-12-20
Method:X-RAY DIFFRACTION (1.93 Å)
Cite:Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase
Acta Crystallogr.,Sect.D, 66, 2010
5I3G
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Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase
Descriptor: Triosephosphate isomerase, glycosomal
Authors:Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J.
Deposit date:2016-02-10
Release date:2016-05-18
Last modified:2023-09-27
Method:X-RAY DIFFRACTION (1.96 Å)
Cite:Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
Biochemistry, 55, 2016
2X1R
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Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase
Descriptor: 3-(PROPYLSULFONYL)PROPANOIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE, ...
Authors:Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Casteleijn, M.G, Neubauer, P, Salmon, L, Wierenga, R.
Deposit date:2010-01-04
Release date:2010-01-26
Last modified:2023-12-20
Method:X-RAY DIFFRACTION (1.98 Å)
Cite:Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase
Acta Crystallogr.,Sect.D, 66, 2010
2VEN
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BU of 2ven by Molmil
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
2J24
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The functional role of the conserved active site proline of triosephosphate isomerase
Descriptor: TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL
Authors:Casteleijn, M.G, Alahuhta, M, Groebel, K, El-Sayed, I, Augustyns, K, Lambeir, A.M, Neubauer, P, Wierenga, R.K.
Deposit date:2006-08-16
Release date:2007-01-02
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase.
Biochemistry, 45, 2006
2WSQ
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BU of 2wsq by Molmil
MonoTIM mutant RMM0-1, dimeric form.
Descriptor: SULFATE ION, TRIOSE PHOSPHATE ISOMERASE, GLYCOSOMAL
Authors:Rudino-Pinera, E, Rojas-Trejo, S.P, Arreola, R, Saab-Rincon, G, Soberon, X, Horjales, E.
Deposit date:2009-09-08
Release date:2009-09-15
Last modified:2023-12-20
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Space Group Transition Driven by Temperature and Related to Monomer-Dimer Transition in Solution: The Case of Monomeric Tim of Trypanosoma Brucei Brucei
To be Published
1TPE
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BU of 1tpe by Molmil
COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS
Descriptor: TRIOSEPHOSPHATE ISOMERASE
Authors:Noble, M.E.M, 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 (2.1 Å)
Cite:Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms.
Protein Sci., 3, 1994
1TPD
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BU of 1tpd by Molmil
STRUCTURES OF THE "OPEN" AND "CLOSED" STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM
Descriptor: TRIOSEPHOSPHATE ISOMERASE
Authors:Noble, M.E.M, 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 (2.1 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, 16, 1993
2X16
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Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase
Descriptor: TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL
Authors:Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Casteleijn, M.G, Neubauer, P, Salmon, L, Wierenga, R.
Deposit date:2009-12-21
Release date:2009-12-29
Last modified:2023-12-20
Method:X-RAY DIFFRACTION (2.13 Å)
Cite:Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase
Acta Crystallogr.,Sect.D, 66, 2010

 

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