1IIH
 
 | | STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHOGLYCERATE | | Descriptor: | 3-PHOSPHOGLYCERIC ACID, TRIOSEPHOSPHATE ISOMERASE | | Authors: | Noble, M.E, Wierenga, R.K, Lambeir, A.M, Opperdoes, F.R, Thunnissen, A.M, Kalk, K.H, Groendijk, H, Hol, W.G.J. | | Deposit date: | 2001-04-23 | | Release date: | 2001-05-11 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes.
Proteins, 10, 1991
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1KV5
 | | 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
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1M1T
 | | Biosynthetic thiolase, Q64A mutant | | Descriptor: | Acetyl-CoA acetyltransferase, GLYCEROL, SULFATE ION | | Authors: | Kursula, P, Ojala, J, Lambeir, A.-M, Wierenga, R.K. | | Deposit date: | 2002-06-20 | | Release date: | 2002-11-29 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (1.94 Å) | | Cite: | The catalytic cycle of biosynthetic thiolase: A conformational
journey of an acetyl group through four binding modes and two oxyanion holes
Biochemistry, 41, 2002
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1M3Z
 | | Biosynthetic thiolase, C89A mutant, complexed with acetyl coenzyme A | | Descriptor: | ACETYL COENZYME *A, Acetyl-CoA acetyltransferase, SULFATE ION | | Authors: | Kursula, P, Ojala, J, Lambeir, A.-M, Wierenga, R.K. | | Deposit date: | 2002-07-03 | | Release date: | 2002-11-29 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (1.87 Å) | | Cite: | The catalytic cycle of biosynthetic thiolase: A conformational
journey of an acetyl group through four binding modes and two oxyanion holes
Biochemistry, 41, 2002
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2V5L
 | | 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: | 2024-05-08 | | 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
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4ZDB
 | | Yeast enoyl-CoA isomerase (ScECI2) complexed with acetoacetyl-CoA | | Descriptor: | 3,2-trans-enoyl-CoA isomerase, ACETOACETYL-COENZYME A, GLYCEROL, ... | | Authors: | Onwukwe, G.U, Koski, M.K, Wierenga, R.K. | | Deposit date: | 2015-04-17 | | Release date: | 2015-11-11 | | Last modified: | 2024-01-10 | | Method: | X-RAY DIFFRACTION (2.14 Å) | | Cite: | Structures of yeast peroxisomal Delta (3), Delta (2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole.
Acta Crystallogr.,Sect.D, 71, 2015
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4ZDF
 | | Crystal structure of yeast enoyl-CoA isomerase helix-10 deletion (ScECI2-H10) mutant | | Descriptor: | 3,2-trans-enoyl-CoA isomerase, GLYCEROL | | Authors: | Onwukwe, G.U, Koski, M.K, Wierenga, R.K. | | Deposit date: | 2015-04-17 | | Release date: | 2015-11-11 | | Last modified: | 2024-01-10 | | Method: | X-RAY DIFFRACTION (1.81 Å) | | Cite: | Structures of yeast peroxisomal Delta (3), Delta (2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole.
Acta Crystallogr.,Sect.D, 71, 2015
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4ZDE
 | | Crystal structure of yeast D3,D2-enoyl-CoA isomerase F268A mutant | | Descriptor: | 3,2-trans-enoyl-CoA isomerase, GLYCEROL, SULFATE ION | | Authors: | Onwukwe, G.U, Koski, M.K, Wierenga, R.K. | | Deposit date: | 2015-04-17 | | Release date: | 2015-11-11 | | Last modified: | 2024-01-10 | | Method: | X-RAY DIFFRACTION (2.1 Å) | | Cite: | Structures of yeast peroxisomal Delta (3), Delta (2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole.
Acta Crystallogr.,Sect.D, 71, 2015
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4ZDD
 | | Structure of yeast D3,D2-enoyl-CoA isomerase bound to sulphate ion | | Descriptor: | 3,2-trans-enoyl-CoA isomerase, SULFATE ION | | Authors: | Onwukwe, G.U, Koski, M.K, Wierenga, R.K. | | Deposit date: | 2015-04-17 | | Release date: | 2015-11-11 | | Last modified: | 2024-01-10 | | Method: | X-RAY DIFFRACTION (3 Å) | | Cite: | Structures of yeast peroxisomal Delta (3), Delta (2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole.
Acta Crystallogr.,Sect.D, 71, 2015
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4ZDC
 | | Yeast enoyl-CoA isomerase complexed with octanoyl-CoA | | Descriptor: | 3,2-trans-enoyl-CoA isomerase, GLYCEROL, OCTANOYL-COENZYME A, ... | | Authors: | Onwukwe, G.U, Koski, M.K, Wierenga, R.K. | | Deposit date: | 2015-04-17 | | Release date: | 2015-11-11 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (2.13 Å) | | Cite: | Structures of yeast peroxisomal Delta (3), Delta (2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole.
Acta Crystallogr.,Sect.D, 71, 2015
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4B3J
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4B3I
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4BT9
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4BT8
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4BTA
 | | CRYSTAL STRUCTURE OF THE PEPTIDE(PRO-PRO-GLY)3 BOUND COMPLEX OF N- TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE (RESIDUES 1-244) TYPE I FROM HUMAN | | Descriptor: | PROLINE RICH PEPTIDE, PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-1 | | Authors: | Anantharajan, J, Koski, M.K, Pekkala, M, Wierenga, R.K. | | Deposit date: | 2013-06-14 | | Release date: | 2013-10-09 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (2.95 Å) | | Cite: | The Structural Motifs for Substrate Binding and Dimerization of the Alpha Subunit of Collagen Prolyl 4-Hydroxylase
Structure, 21, 2013
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4CQM
 | | Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP | | Descriptor: | 1,2-ETHANEDIOL, ACETATE ION, CARBONYL REDUCTASE FAMILY MEMBER 4, ... | | Authors: | Venkatesan, R, SahTeli, S.K, Awoniyi, L.O, Jiang, G, Prus, P, Kastoniotis, A.J, Hiltunen, J.K, Wierenga, R.K, Chen, Z. | | Deposit date: | 2014-02-19 | | Release date: | 2014-09-10 | | Last modified: | 2014-09-17 | | Method: | X-RAY DIFFRACTION (2.339 Å) | | Cite: | Insights Into Mitochondrial Fatty Acid Synthesis from the Structure of Heterotetrameric 3-Ketoacyl-Acp Reductase/3R-Hydroxyacyl-Coa Dehydrogenase.
Nat.Commun., 5, 2014
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4BTB
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6TNM
 | | E. coli aerobic trifunctional enzyme subunit-alpha | | Descriptor: | ADENOSINE-5'-TRIPHOSPHATE, Fatty acid oxidation complex subunit alpha, GLYCEROL, ... | | Authors: | Sah-Teli, S.K, Hynonen, M.J, Wierenga, R.K, Venkatesan, R. | | Deposit date: | 2019-12-09 | | Release date: | 2020-03-25 | | Last modified: | 2024-01-24 | | Method: | X-RAY DIFFRACTION (2.95 Å) | | Cite: | Insights into the stability and substrate specificity of the E. coli aerobic beta-oxidation trifunctional enzyme complex.
J.Struct.Biol., 210, 2020
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4CQL
 | | Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD | | Descriptor: | CARBONYL REDUCTASE FAMILY MEMBER 4, ESTRADIOL 17-BETA-DEHYDROGENASE 8, NICOTINAMIDE-ADENINE-DINUCLEOTIDE | | Authors: | Venkatesan, R, Sah-Teli, S.K, Awoniyi, L.O, Jiang, G, Prus, P, Kastaniotis, A.J, Hiltunen, J.K, Wierenga, R.K, Chen, Z. | | Deposit date: | 2014-02-19 | | Release date: | 2014-09-10 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (2.85 Å) | | Cite: | Insights Into Mitochondrial Fatty Acid Synthesis from the Structure of Heterotetrameric 3-Ketoacyl-Acp Reductase/3R-Hydroxyacyl-Coa Dehydrogenase.
Nat.Commun., 5, 2014
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2VCY
 | | Crystal Structure of 2-Enoyl Thioester Reductase of Human FAS II | | Descriptor: | SULFATE ION, TRANS-2-ENOYL-COA REDUCTASE | | Authors: | Haapalainen, A.M, Pudas, R, Smart, O.S, Wierenga, R.K. | | Deposit date: | 2007-09-28 | | Release date: | 2008-06-03 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (2.41 Å) | | Cite: | Structural Enzymological Studies of 2-Enoyl Thioester Reductase of the Human Mitochondrial Fas II Pathway: New Insights Into its Substrate Recognition Properties.
J.Mol.Biol., 379, 2008
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2V2H
 | | 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
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2VU0
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2VEK
 | | 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
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2VEI
 | | 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
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2VU2
 | | Biosynthetic thiolase from Z. ramigera. Complex with S-pantetheine-11- pivalate. | | Descriptor: | (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate, ACETYL-COA ACETYLTRANSFERASE, SULFATE ION | | Authors: | Kursula, P, Merilainen, G, Schmitz, W, Wierenga, R.K. | | Deposit date: | 2008-05-19 | | Release date: | 2008-10-28 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (2.65 Å) | | Cite: | The Sulfur Atoms of the Substrate Coa and the Catalytic Cysteine are Required for a Productive Mode of Substrate Binding in Bacterial Biosynthetic Thiolase, a Thioester-Dependent Enzyme.
FEBS J., 275, 2008
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