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1XYL
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THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID
Descriptor:XYLOSE ISOMERASE, MAGNESIUM ION, HYDROXIDE ION
Authors:Allen, K.N., Lavie, A., Petsko, G.A., Ringe, D.
Deposit date:1993-12-07
Release date:1994-05-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acid.
Biochemistry, 33, 1994
1XYM
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THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID
Descriptor:XYLOSE ISOMERASE, D-GLUCOSE IN LINEAR FORM, MAGNESIUM ION, ...
Authors:Allen, K.N., Lavie, A., Petsko, G.A., Ringe, D.
Deposit date:1993-12-07
Release date:1994-05-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acid.
Biochemistry, 33, 1994
2GYI
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DESIGN, SYNTHESIS, AND CHARACTERIZATION OF A POTENT XYLOSE ISOMERASE INHIBITOR, D-THREONOHYDROXAMIC ACID, AND HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHIC STRUCTURE OF THE ENZYME-INHIBITOR COMPLEX
Descriptor:XYLOSE ISOMERASE, MAGNESIUM ION, 2,3,4,N-TETRAHYDROXY-BUTYRIMIDIC ACID
Authors:Allen, K.N., Lavie, A., Petsko, G.A., Ringe, D.
Deposit date:1994-09-01
Release date:1995-07-10
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.6 Å)
Cite:Design, Synthesis, and Characterization of a Potent Xylose Isomerase Inhibitor, D-Threonohydroxamic Acid, and High-Resolution X-Ray Crystallographic Structure of the Enzyme-Inhibitor Complex
Biochemistry, 34, 1995
1TPB
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OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE
Descriptor:TRIOSEPHOSPHATE ISOMERASE, PHOSPHOGLYCOLOHYDROXAMIC ACID
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:2011-07-13
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
1TPC
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OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE
Descriptor:TRIOSEPHOSPHATE ISOMERASE, PHOSPHOGLYCOLOHYDROXAMIC ACID
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:2011-07-13
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
1ASA
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THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
Descriptor:ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, MALEIC ACID
Authors:Schumacher, C., Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:The Structural Basis for the Reduced Activity of the Y226F(Y225F) Active Site Mutant of E. Coli Aspartate Aminotransferase
To be Published
1DAA
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CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE
Descriptor:D-AMINO ACID AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE
Authors:Sugio, S., Peisach, D., Ringe, D.
Deposit date:1995-06-09
Release date:1995-09-15
Last modified:2018-04-04
Method:X-RAY DIFFRACTION (1.94 Å)
Cite:Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity.
Biochemistry, 34, 1995
1XYA
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X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS
Descriptor:XYLOSE ISOMERASE, MAGNESIUM ION, HYDROXIDE ION
Authors:Lavie, A., Allen, K.N., Petsko, G.A., Ringe, D.
Deposit date:1994-01-03
Release date:1994-05-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.81 Å)
Cite:X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis.
Biochemistry, 33, 1994
1XYB
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X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS
Descriptor:XYLOSE ISOMERASE, D-GLUCOSE IN LINEAR FORM, MAGNESIUM ION
Authors:Lavie, A., Allen, K.N., Petsko, G.A., Ringe, D.
Deposit date:1994-01-03
Release date:1994-05-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.96 Å)
Cite:X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis.
Biochemistry, 33, 1994
1XYC
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X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS
Descriptor:XYLOSE ISOMERASE, 3-O-METHYLFRUCTOSE IN LINEAR FORM, MAGNESIUM ION
Authors:Lavie, A., Allen, K.N., Petsko, G.A., Ringe, D.
Deposit date:1994-01-03
Release date:1994-05-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (2.19 Å)
Cite:X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis.
Biochemistry, 33, 1994
3FZW
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CRYSTAL STRUCTURE OF KETOSTEROID ISOMERASE D40N-D103N FROM PSEUDOMONAS PUTIDA (PKSI) WITH BOUND EQUILENIN
Descriptor:Steroid Delta-isomerase, EQUILENIN, GLYCEROL, ...
Authors:Caaveiro, J.M.M., Ringe, D., Petsko, G.A.
Deposit date:2009-01-26
Release date:2009-06-02
Last modified:2017-11-01
Method:X-RAY DIFFRACTION (1.32 Å)
Cite:Hydrogen bond coupling in the ketosteroid isomerase active site.
Biochemistry, 48, 2009
2DAA
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CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY D-CYCLOSERINE
Descriptor:D-AMINO ACID AMINOTRANSFERASE, D-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-N,O-CYCLOSERYLAMIDE
Authors:Peisach, D., Chipman, D.M., Ringe, D.
Deposit date:1997-10-27
Release date:1998-03-18
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:D-Cycloserine Inactivation of D-Amino Acid Aminotransferase Leads to a Stable Noncovalent Protein Complex with an Aromatic Cycloserine-Plp Derivative
J.Am.Chem.Soc., 120, 1998
3DAA
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CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY PYRIDOXYL-D-ALANINE
Descriptor:D-AMINO ACID AMINOTRANSFERASE, N-(5'-PHOSPHOPYRIDOXYL)-D-ALANINE
Authors:Peisach, D., Chipman, D.M., Ringe, D.
Deposit date:1998-01-20
Release date:1998-04-29
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase.
Biochemistry, 37, 1998
4DAA
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CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE IN PYRIDOXAL-5'-PHOSPHATE (PLP) FORM
Descriptor:D-AMINO ACID AMINOTRANSFERASE, SULFATE ION, PYRIDOXAL-5'-PHOSPHATE
Authors:Peisach, D., Chipman, D.M., Ringe, D.
Deposit date:1998-01-26
Release date:1998-04-29
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase.
Biochemistry, 37, 1998
1G2W
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E177S MUTANT OF THE PYRIDOXAL-5'-PHOSPHATE ENZYME D-AMINO ACID AMINOTRANSFERASE
Descriptor:D-ALANINE AMINOTRANSFERASE, ACETATE ION, PYRIDOXAL-5'-PHOSPHATE
Authors:Lepore, B.W., Ringe, D.
Deposit date:2000-10-21
Release date:2000-11-15
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2 Å)
Cite:Studies on an Active Site Residue, E177, That Affects Binding of the Coenzyme in D-Amino Acid Transaminase, and Mechanistic Studies on a Suicide Substrate
Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins, 10th Annual International Symposium on Vitamin B6, 2000
2INX
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CRYSTAL STRUCTURE OF KETOSTEROID ISOMERASE D40N FROM PSEUDOMONAS PUTIDA (PKSI) WITH BOUND 2,6-DIFLUOROPHENOL
Descriptor:Steroid delta-isomerase, 2,6-DIFLUOROPHENOL
Authors:Martinez Caaveiro, J.M., Pybus, B., Ringe, D., Petsko, G.A., Sigala, P., Kraut, D., Herschlag, D.
Deposit date:2006-10-09
Release date:2007-10-23
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (1.5 Å)
Cite:Testing geometrical discrimination within an enzyme active site: constrained hydrogen bonding in the ketosteroid isomerase oxyanion hole.
J.Am.Chem.Soc., 130, 2008
1A0G
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L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAMINE-5'-PHOSPHATE
Descriptor:D-AMINO ACID AMINOTRANSFERASE, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE
Authors:Sugio, S., Kashima, A., Kishimoto, K., Peisach, D., Petsko, G.A., Ringe, D., Yoshimura, T., Esaki, N.
Deposit date:1997-11-30
Release date:1998-06-03
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2 Å)
Cite:Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination.
Protein Eng., 11, 1998
1AAM
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THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE R292D ACTIVE SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM E. COLI
Descriptor:ASPARTATE AMINOTRANSFERASE, SULFATE ION, PYRIDOXAL-5'-PHOSPHATE
Authors:Almo, S.C., Smith, D.L., Danishefsky, A.T., Ringe, D.
Deposit date:1993-07-13
Release date:1993-10-31
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli.
Protein Eng., 7, 1994
1AAW
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THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE R292D ACTIVE SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM E. COLI
Descriptor:ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE
Authors:Almo, S.C., Smith, D.L., Danishefsky, A.T., Ringe, D.
Deposit date:1993-07-13
Release date:1993-10-31
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli.
Protein Eng., 7, 1994
1ASB
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THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE D223A(D222A) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
Descriptor:ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, MALEIC ACID
Authors:Schumacher, C., Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2012-07-25
Method:X-RAY DIFFRACTION (2.6 Å)
Cite:The Structural Basis for the Reduced Activity of the D223A(D222A) Active Site Mutant of E. Coli Aspartate Aminotransferase
To be Published
1ASC
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THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE D223A(D222A) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
Descriptor:ASPARTATE AMINOTRANSFERASE, N-METHYL-4-DEOXY-4-AMINO-PYRIDOXAL-5-PHOSPHATE
Authors:Schumacher, C., Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2012-07-25
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:The Structural Basis for the Reduced Activity of the D223A(D222A) Active Site Mutant of E. Coli Aspartate Aminotransferase
To be Published
1ASD
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THE STRUCTURE OF WILD TYPE E. COLI ASPARTATE AMINOTRANSFERASE RECONSTITUTED WITH N-MEPLP
Descriptor:ASPARTATE AMINOTRANSFERASE, N-METHYL-PYRIDOXAL-5'-PHOSPHATE, MALEIC ACID
Authors:Schumacher, C., Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:The Structure of Wild Type E. Coli Aspartate Aminotransferase Reconstituted with N-Meplp
To be Published
1ASE
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THE STRUCTURE OF WILD TYPE E. COLI ASPARTATE AMINOTRANSFERASE RECONSTITUTED WITH PLP-N-OXIDE
Descriptor:ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE-N-OXIDE, MALEIC ACID
Authors:Schumacher, C., Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:The Structure of Wild Type E. Coli Aspartate Aminotransferase Reconstituted with Plp-N-Oxide
To be Published
1ASF
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THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
Descriptor:ASPARTATE AMINOTRANSFERASE, SULFATE ION, PYRIDOXAL-5'-PHOSPHATE
Authors:Schumacher, C., Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2012-07-25
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:The Structural Basis for the Reduced Activity of the Y226F(Y225F) Active Site Mutant of E. Coli Aspartate Aminotransferase
To be Published
1ASG
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THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
Descriptor:ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, MALEIC ACID
Authors:Schumacher, C., Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2012-07-25
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:The Structural Basis for the Reduced Activity of the Y226F(Y225F) Active Site Mutant of E. Coli Aspartate Aminotransferase
To be Published