2VEN
| 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
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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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2VEL
| 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: | 2-PHOSPHOGLYCOLIC ACID, CHLORIDE ION, 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: | 2007-10-24 | Release date: | 2008-02-19 | Last modified: | 2024-05-01 | Method: | X-RAY DIFFRACTION (2.3 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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2VEM
| 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: | 2024-10-16 | 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
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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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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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2VXN
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2V0T
| 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
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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
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2V2C
| 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
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1FMF
| REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM TETANOMORPHUM | Descriptor: | METHYLASPARTATE MUTASE S CHAIN | Authors: | Hoffmann, B, Konrat, R, Tollinger, M, Huhta, M, Marsh, E.N.G, Kraeutler, B. | Deposit date: | 2000-08-17 | Release date: | 2002-02-15 | Last modified: | 2024-05-01 | Method: | SOLUTION NMR | Cite: | A protein pre-organized to trap the nucleotide moiety of coenzyme B(12): refined solution structure of the B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum. Chembiochem, 2, 2001
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2J24
| 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
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2J27
| 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
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2Y63
| Crystal structure of Leishmanial E65Q-TIM complexed with Bromohydroxyacetone phosphate | Descriptor: | (3-bromo-2-oxo-propoxy)phosphonic acid, TRIOSEPHOSPHATE ISOMERASE | Authors: | Venkatesan, R, Alahuhta, M, Pihko, P.M, Wierenga, R.K. | Deposit date: | 2011-01-19 | Release date: | 2011-12-14 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (1.97 Å) | Cite: | High Resolution Crystal Structures of Triosephosphate Isomerase Complexed with its Suicide Inhibitors: The Conformational Flexibility of the Catalytic Glutamate in its Closed, Liganded Active Site. Protein Sci., 20, 2011
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2Y62
| Crystal structure of Leishmanial E65Q-TIM complexed with R-Glycidol phosphate | Descriptor: | GLYCEROL, SN-GLYCEROL-1-PHOSPHATE, SN-GLYCEROL-3-PHOSPHATE, ... | Authors: | Venkatesan, R, Alahuhta, M, Pihko, P.M, Wierenga, R.K. | Deposit date: | 2011-01-19 | Release date: | 2011-12-14 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (1.08 Å) | Cite: | High Resolution Crystal Structures of Triosephosphate Isomerase Complexed with its Suicide Inhibitors: The Conformational Flexibility of the Catalytic Glutamate in its Closed, Liganded Active Site. Protein Sci., 20, 2011
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2Y61
| Crystal structure of Leishmanial E65Q-TIM complexed with S-Glycidol phosphate | Descriptor: | GLYCEROL, SN-GLYCEROL-1-PHOSPHATE, SN-GLYCEROL-3-PHOSPHATE, ... | Authors: | Venkatesan, R, Alahuhta, M, Pihko, P.M, Wierenga, R.K. | Deposit date: | 2011-01-19 | Release date: | 2011-12-14 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (0.99 Å) | Cite: | High resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: the conformational flexibility of the catalytic glutamate in its closed, liganded active site. Protein Sci., 20, 2011
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3MPC
| The crystal structure of a Fn3-like protein from Clostridium thermocellum | Descriptor: | Fn3-like protein, SULFATE ION | Authors: | Alahuhta, M.P, Xu, Q, Brunecky, R, Lunin, V.V. | Deposit date: | 2010-04-26 | Release date: | 2010-08-11 | Last modified: | 2024-02-21 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | Structure of a fibronectin type III-like module from Clostridium thermocellum. Acta Crystallogr.,Sect.F, 66, 2010
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3K4Z
| Crystal Structure of the Cellulosomal CBM4 from Clostridium thermocellum Cellulase CbhA | Descriptor: | 1-O-phosphono-beta-D-glucopyranose, Glycoside hydrolase family 9, MAGNESIUM ION, ... | Authors: | Alahuhta, P.M, Xu, Q, Himmel, M.E, Lunin, V.V. | Deposit date: | 2009-10-06 | Release date: | 2010-07-28 | Last modified: | 2023-09-06 | Method: | X-RAY DIFFRACTION (2.11 Å) | Cite: | The unique binding mode of cellulosomal CBM4 from Clostridium thermocellum cellobiohydrolase A. J.Mol.Biol., 402, 2010
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3T9G
| The crystal structure of family 3 pectate lyase from Caldicellulosiruptor bescii | Descriptor: | (4R)-2-METHYLPENTANE-2,4-DIOL, (4S)-2-METHYL-2,4-PENTANEDIOL, 1,2-ETHANEDIOL, ... | Authors: | Alahuhta, P.M, Lunin, V.V. | Deposit date: | 2011-08-02 | Release date: | 2012-05-09 | Last modified: | 2023-09-13 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | A 1.5 A resolution X-ray structure of the catalytic module of Caldicellulosiruptor bescii family 3 pectate lyase. Acta Crystallogr.,Sect.F, 67, 2011
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4LGN
| The structure of Acidothermus cellulolyticus family 74 glycoside hydrolase | Descriptor: | 1,2-ETHANEDIOL, ACETATE ION, Cellulose-binding, ... | Authors: | Alahuhta, P.M, Lunin, V.V. | Deposit date: | 2013-06-28 | Release date: | 2013-12-11 | Last modified: | 2023-09-20 | Method: | X-RAY DIFFRACTION (1.82 Å) | Cite: | Structure of Acidothermus cellulolyticus family 74 glycoside hydrolase at 1.82 angstrom resolution. Acta Crystallogr.,Sect.F, 69, 2013
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3P6B
| The crystal structure of CelK CBM4 from Clostridium thermocellum | Descriptor: | ACETATE ION, CALCIUM ION, Cellulose 1,4-beta-cellobiosidase, ... | Authors: | Alahuhta, P.M, Luo, Y, Lunin, V.V. | Deposit date: | 2010-10-11 | Release date: | 2011-08-24 | Last modified: | 2023-09-06 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Structure of CBM4 from Clostridium thermocellum cellulase K. Acta Crystallogr.,Sect.F, 67, 2011
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4EW9
| The liganded structure of C. bescii family 3 pectate lyase | Descriptor: | (4S)-2-METHYL-2,4-PENTANEDIOL, 4-deoxy-beta-L-threo-hex-4-enopyranuronic acid-(1-4)-alpha-D-galactopyranuronic acid, ACETATE ION, ... | Authors: | Alahuhta, P.M, Lunin, V.V. | Deposit date: | 2012-04-26 | Release date: | 2013-03-20 | Last modified: | 2023-09-13 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | The structure and mode of action of Caldicellulosiruptor bescii family 3 pectate lyase in biomass deconstruction. Acta Crystallogr. D Biol. Crystallogr., 69, 2013
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4Z06
| C. bescii Family 3 pectate lyase double mutant K108A/R133A in complex with ALPHA-D-GALACTOPYRANURONIC ACID | Descriptor: | (4R)-2-METHYLPENTANE-2,4-DIOL, (4S)-2-METHYL-2,4-PENTANEDIOL, CALCIUM ION, ... | Authors: | Alahuhta, P.M, Lunin, V.V. | Deposit date: | 2015-03-25 | Release date: | 2015-12-23 | Last modified: | 2024-03-06 | Method: | X-RAY DIFFRACTION (1.55 Å) | Cite: | The catalytic mechanism and unique low pH optimum of Caldicellulosiruptor bescii family 3 pectate lyase. Acta Crystallogr.,Sect.D, 71, 2015
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4Z05
| C. bescii Family 3 pectate lyase mutant E84A | Descriptor: | (4R)-2-METHYLPENTANE-2,4-DIOL, (4S)-2-METHYL-2,4-PENTANEDIOL, CALCIUM ION, ... | Authors: | Alahuhta, P.M, Lunin, V.V. | Deposit date: | 2015-03-25 | Release date: | 2015-12-23 | Last modified: | 2019-12-04 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | The catalytic mechanism and unique low pH optimum of Caldicellulosiruptor bescii family 3 pectate lyase. Acta Crystallogr.,Sect.D, 71, 2015
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4YZA
| C. bescii Family 3 pectate lyase double mutant K108A/Q111A in complex with trigalacturonic acid | Descriptor: | (4R)-2-METHYLPENTANE-2,4-DIOL, (4S)-2-METHYL-2,4-PENTANEDIOL, CALCIUM ION, ... | Authors: | Alahuhta, P.M, Lunin, V.V. | Deposit date: | 2015-03-24 | Release date: | 2015-12-23 | Last modified: | 2020-07-29 | Method: | X-RAY DIFFRACTION (1.25 Å) | Cite: | The catalytic mechanism and unique low pH optimum of Caldicellulosiruptor bescii family 3 pectate lyase. Acta Crystallogr.,Sect.D, 71, 2015
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