2V2D
 
 | | 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: | PHOSPHATE 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 (2.3 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
|
|
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: | 2023-12-13 | | 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
|
|
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
|
|
1SU5
 | | Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase | | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, GLYCEROL, SULFATE ION, ... | | Authors: | Kursula, I, Salin, M, Sun, J, Norledge, B.V, Haapalainen, A.M, Sampson, N.S, Wierenga, R.K. | | Deposit date: | 2004-03-26 | | Release date: | 2004-08-24 | | Last modified: | 2023-10-25 | | Method: | X-RAY DIFFRACTION (2.7 Å) | | Cite: | Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase
Protein Eng.Des.Sel., 17, 2004
|
|
1SW7
 | | Triosephosphate isomerase from Gallus gallus, loop 6 mutant K174N, T175S, A176S | | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, Triosephosphate isomerase | | Authors: | Kursula, I, Salin, M, Sun, J, Norledge, B.V, Haapalainen, A.M, Sampson, N.S, Wierenga, R.K. | | Deposit date: | 2004-03-30 | | Release date: | 2004-08-24 | | Last modified: | 2023-10-25 | | Method: | X-RAY DIFFRACTION (2.22 Å) | | Cite: | Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase
Protein Eng.Des.Sel., 17, 2004
|
|
1TJC
 | | Crystal structure of peptide-substrate-binding domain of human type I collagen prolyl 4-hydroxylase | | Descriptor: | Prolyl 4-hydroxylase alpha-1 subunit | | Authors: | Pekkala, M, Hieta, R, Bergmann, U, Kivirikko, K.I, Wierenga, R.K, Myllyharju, J. | | Deposit date: | 2004-06-04 | | Release date: | 2004-10-12 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.3 Å) | | Cite: | The Peptide-Substrate-binding Domain of Collagen Prolyl 4-Hydroxylases Is a Tetratricopeptide Repeat Domain with Functional Aromatic Residues.
J.Biol.Chem., 279, 2004
|
|
1TJ7
 | | Structure determination and refinement at 2.44 A resolution of Argininosuccinate lyase from E. coli | | Descriptor: | Argininosuccinate lyase, GLYCEROL, PHOSPHATE ION | | Authors: | Bhaumik, P, Koski, M.K, Bergman, U, Wierenga, R.K. | | Deposit date: | 2004-06-03 | | Release date: | 2004-10-26 | | Last modified: | 2023-08-23 | | Method: | X-RAY DIFFRACTION (2.44 Å) | | Cite: | Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli.
Acta Crystallogr.,Sect.D, 60, 2004
|
|
1TMH
 | |
2VXN
 | |
2VU1
 | | Biosynthetic thiolase from Z. ramigera. Complex of with O-pantheteine- 11-pivalate. | | Descriptor: | ACETYL-COA ACETYLTRANSFERASE, PANTOTHENYL-AMINOETHANOL-11-PIVALIC ACID, SODIUM ION, ... | | Authors: | Kursula, P, Schmitz, W, Wierenga, R.K. | | Deposit date: | 2008-05-19 | | Release date: | 2008-10-28 | | Last modified: | 2019-07-24 | | Method: | X-RAY DIFFRACTION (1.51 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
|
|
2VU0
 | |
1TRD
 | |
1TPD
 | |
1TPE
 | |
1TRE
 | |
2VTZ
 | | Biosynthetic thiolase from Z. ramigera. Complex of the C89A mutant with coenzyme A. | | Descriptor: | ACETYL-COA ACETYLTRANSFERASE, COENZYME A, SULFATE ION | | Authors: | Kursula, P, Merilainen, G, Wierenga, R.K. | | Deposit date: | 2008-05-19 | | Release date: | 2008-10-28 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (2.3 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
|
|
1IIG
 | | STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHONOPROPIONATE | | Descriptor: | 3-PHOSPHONOPROPANOIC 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 (2.6 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
|
|
1TPF
 | |
1IF2
 | | X-RAY STRUCTURE OF LEISHMANIA MEXICANA TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH IPP | | Descriptor: | TRIOSEPHOSPHATE ISOMERASE, [2(FORMYL-HYDROXY-AMINO)-ETHYL]-PHOSPHONIC ACID | | Authors: | Kursula, I, Partanen, S, Lambeir, A.-M, Antonov, D.M, Augustyns, K, Wierenga, R.K. | | Deposit date: | 2001-04-12 | | Release date: | 2001-08-17 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | Structural determinants for ligand binding and catalysis of triosephosphate isomerase.
Eur.J.Biochem., 268, 2001
|
|
1TTI
 | |
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
|
|
2X58
 | | The crystal structure of MFE1 liganded with CoA | | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, COENZYME A, GLYCEROL, ... | | Authors: | Kasaragod, P, Venkatesan, R, Kiema, T.R, Hiltunen, J.K, Wierenga, R.K. | | Deposit date: | 2010-02-05 | | Release date: | 2010-05-12 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (2.8 Å) | | Cite: | The Crystal Structure of Liganded Rat Peroxisomal Multifunctional Enzyme Type 1: A Flexible Molecule with Two Interconnected Active Sites
J.Biol.Chem., 285, 2010
|
|
2WKU
 | | BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. THE N316H MUTANT. | | Descriptor: | ACETYL-COA ACETYLTRANSFERASE, D-mannose, SULFATE ION | | Authors: | Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K. | | Deposit date: | 2009-06-18 | | Release date: | 2009-11-03 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (2.3 Å) | | Cite: | The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation.
Biochemistry, 48, 2009
|
|
2WL4
 | | BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE H348A MUTANT WITH COENZYME A. | | Descriptor: | ACETYL-COA ACETYLTRANSFERASE, CHLORIDE ION, COENZYME A, ... | | Authors: | Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K. | | Deposit date: | 2009-06-22 | | Release date: | 2009-11-03 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation.
Biochemistry, 48, 2009
|
|
2WKT
 | | BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE N316A MUTANT WITH COENZYME A. | | Descriptor: | ACETYL-COA ACETYLTRANSFERASE, CHLORIDE ION, COENZYME A, ... | | Authors: | Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K. | | Deposit date: | 2009-06-18 | | Release date: | 2009-11-03 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation.
Biochemistry, 48, 2009
|
|
