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Yorodumi- PDB-1acm: ARGININE 54 IN THE ACTIVE SITE OF ESCHERICHIA COLI ASPARTATE TRAN... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1acm | ||||||
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Title | ARGININE 54 IN THE ACTIVE SITE OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE IS CRITICAL FOR CATALYSIS: A SITE-SPECIFIC MUTAGENESIS, NMR AND X-RAY CRYSTALLOGRAPHY STUDY | ||||||
Components |
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Keywords | TRANSFERASE (CARBAMOYL-P / ASPARTATE) | ||||||
Function / homology | Function and homology information aspartate carbamoyltransferase complex / pyrimidine nucleotide biosynthetic process / aspartate carbamoyltransferase / aspartate carbamoyltransferase activity / amino acid binding / glutamine metabolic process / protein homotrimerization / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process / zinc ion binding ...aspartate carbamoyltransferase complex / pyrimidine nucleotide biosynthetic process / aspartate carbamoyltransferase / aspartate carbamoyltransferase activity / amino acid binding / glutamine metabolic process / protein homotrimerization / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process / zinc ion binding / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.8 Å | ||||||
Authors | Stevens, R.C. / Kantrowitz, E.R. / Lipscomb, W.N. | ||||||
Citation | Journal: Protein Sci. / Year: 1992 Title: Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study. Authors: Stebbins, J.W. / Robertson, D.E. / Roberts, M.F. / Stevens, R.C. / Lipscomb, W.N. / Kantrowitz, E.R. #1: Journal: Biochemistry / Year: 1990 Title: Structural Consequences of Effector Binding to the T State of Aspartate Carbamoyltransferase: Crystal Structures of the Unligated and ATP-, and Ctp-Complexed Enzymes at 2.6-Angstroms Resolution Authors: Stevens, R.C. / Gouaux, J.E. / Lipscomb, W.N. #2: Journal: Biochemistry / Year: 1990 Title: Crystal Structures of Aspartate Carbamoyltransferase Ligated with Phosphonoacetamide, Malonate, and Ctp or ATP at 2.8-Angstroms Resolution and Neutral Ph Authors: Gouaux, J.E. / Stevens, R.C. / Lipscomb, W.N. #3: Journal: Biochemistry / Year: 1990 Title: Crystal Structures of Phosphonoacetamide Ligated T and Phosphonoacetamide and Malonate Ligated R States of Aspartate Carbamoyltransferase at 2.8-Angstroms Resolution and Neutral Ph Authors: Gouaux, J.E. / Lipscomb, W.N. #4: Journal: Proc.Natl.Acad.Sci.USA / Year: 1989 Title: Structural Transitions in Crystals of Native Aspartate Carbamoyltransferase Authors: Gouaux, J.E. / Lipscomb, W.N. #5: Journal: Biochemistry / Year: 1989 Title: Structure of a Single Amino Acid Mutant of Aspartate Carbamoyltransferase at 2.5-Angstroms Resolution. Implications for the Cooperative Mechanism Authors: Gouaux, J.E. / Lipscomb, W.N. / Middleton, S.A. / Kantrowitz, E.R. #6: Journal: Science / Year: 1988 Title: Escherichia Coli Aspartate Transcarbamylase. The Relation between Structure and Function Authors: Kantrowitz, E.R. / Lipscomb, W.N. #7: Journal: Proc.Natl.Acad.Sci.USA / Year: 1988 Title: Three-Dimensional Structure of Carbamoyl Phosphate and Succinate Bound to Aspartate Carbamoyltransferase Authors: Gouaux, J.E. / Lipscomb, W.N. #8: Journal: J.Mol.Biol. / Year: 1987 Title: Structural Asymmetry in the Ctp-Liganded Form of Aspartate Carbamoyltransferase from Escherichia Coli Authors: Kim, K.H. / Pan, Z. / Honzatko, R.B. / Ke, H. / Lipscomb, W.N. #9: Journal: J.Mol.Biol. / Year: 1987 Title: 2.5 Angstroms Structure of Aspartate Carbamoyltransferase Complexed with the Bisubstrate Analog N-(Phosphonacetyl)-L-Aspartate Authors: Krause, K.L. / Volz, K.W. / Lipscomb, W.N. #10: Journal: Biochem.Biophys.Res.Commun. / Year: 1987 Title: The Catalytic Mechanism of Escherichia Coli Aspartate Carbamoyltransferase. A Molecular Modelling Study Authors: Gouaux, J.E. / Krause, K.L. / Lipscomb, W.N. #11: Journal: Proc.Natl.Acad.Sci.USA / Year: 1985 Title: Structure at 2.9-Angstroms Resolution of Aspartate Carbamoyltransferase Complexed with the Bisubstrate Analogue N-(Phosphonacetyl)-L-Aspartate Authors: Krause, K.L. / Volz, K.W. / Lipscomb, W.N. #12: Journal: Proc.Natl.Acad.Sci.USA / Year: 1984 Title: Structure of Unligated Aspartate Carbamoyltransferase of Escherichia Coli at 2.6-Angstroms Resolution Authors: Ke, H. / Honzatko, R.B. / Lipscomb, W.N. #13: Journal: J.Mol.Biol. / Year: 1982 Title: Crystal and Molecular Structures of Native and Ctp-Liganded Aspartate Carbamoyltransferase from Escherichia Coli Authors: Honzatko, R.B. / Crawford, J.L. / Monaco, H.L. / Ladner, J.E. / Edwards, B.F.P. / Evans, D.R. / Warren, S.G. / Wiley, D.C. / Ladner, R.C. / Lipscomb, W.N. #14: Journal: J.Mol.Biol. / Year: 1982 Title: Interactions of Phosphate Ligands with Escherichia Coli Aspartate Carbamoyltransferase in the Crystalline State Authors: Honzatko, R.B. / Lipscomb, W.N. #15: Journal: Proc.Natl.Acad.Sci.USA / Year: 1982 Title: Interactions of Metal-Nucleotide Complexes with Aspartate Carbamoyltransferase in the Crystalline State Authors: Honzatko, R.B. / Lipscomb, W.N. #16: Journal: Proc.Natl.Acad.Sci.USA / Year: 1982 Title: Gross Quaternary Changes in Aspartate Carbamoyltransferase are Induced by the Binding of N-(Phosphonacetyl)-L-Aspartate. A 3.5-Angstroms Resolution Study Authors: Ladner, J.E. / Kitchell, J.P. / Honzatko, R.B. / Ke, H.M. / Volz, K.W. / Kalb(Gilboa), A.J. / Ladner, R.C. / Lipscomb, W.N. #17: Journal: Proc.Natl.Acad.Sci.USA / Year: 1979 Title: A 3.0-Angstroms Resolution Study of Nucleotide Complexes with Aspartate Carbamoyltransferase Authors: Honzatko, R.B. / Monaco, H.L. / Lipscomb, W.N. #18: Journal: Proc.Natl.Acad.Sci.USA / Year: 1978 Title: Three-Dimensional Structures of Aspartate Carbamoyltransferase from Escherichia Coli and of its Complex with Cytidine Triphosphate Authors: Monaco, H.L. / Crawford, J.L. / Lipscomb, W.N. #19: Journal: STRUCTURE AND CONFORMATION OF NUCLEIC ACIDS AND PROTEIN-NUCLEIC ACID INTERACTIONS : PROCEEDINGS OF THE FOURTH ANNUAL HARRY STEENBOCK SYMPOSIUM, JUNE 16-19, 1974, MADISON, WISCONSIN Year: 1975 Title: Binding Site at 5.5 Angstroms Resolution of Cytidine Triphosphate, the Allosteric Inhibitor of Aspartate Transcarbamylase from Escherichia Coli. Relation to Mechanisms of Control Authors: Lipscomb, W.N. / Edwards, B.F.P. / Evans, D.R. / Pastra-Landis, S.C. #20: Journal: Proc.Natl.Acad.Sci.USA / Year: 1973 Title: Aspartate Transcarbamoylase from Escherichia Coli. Electron Density at 5.5 Angstroms Resolution Authors: Warren, S.G. / Edwards, B.F.P. / Evans, D.R. / Wiley, D.C. / Lipscomb, W.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1acm.cif.gz | 185.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1acm.ent.gz | 149.7 KB | Display | PDB format |
PDBx/mmJSON format | 1acm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1acm_validation.pdf.gz | 488.1 KB | Display | wwPDB validaton report |
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Full document | 1acm_full_validation.pdf.gz | 513.7 KB | Display | |
Data in XML | 1acm_validation.xml.gz | 21.6 KB | Display | |
Data in CIF | 1acm_validation.cif.gz | 32.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ac/1acm ftp://data.pdbj.org/pub/pdb/validation_reports/ac/1acm | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUES PRO A 268 AND PRO C 268 ARE CIS-PROLINES. | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.105647, -0.993868, 0.03264), Vector: Details | THE NON-CRYSTALLOGRAPHIC TWO-FOLD AXIS, WHICH IS SPECIFIED ON THE *MTRIX* RECORDS BELOW, RELATES THE *A* AND *B* CHAINS TO THE *C* AND *D* CHAINS. | |
-Components
#1: Protein | Mass: 34250.992 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source References: UniProt: P0A786, aspartate carbamoyltransferase #2: Protein | Mass: 17072.549 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source References: UniProt: P0A7F3 #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | Compound details | ACTIVE BINDING CATALYTIC CHAIN (CHAINS A AND C) RESIDUE ARGININE 54 IN THE ACTIVE BINDING SITE HAS ...ACTIVE BINDING CATALYTIC CHAIN (CHAINS A AND C) RESIDUE ARGININE 54 IN THE ACTIVE BINDING SITE HAS BEEN REPLACED WITH ALANINE BY SITE-SPECIFIC MUTAGENESI | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.28 Å3/Da / Density % sol: 62.48 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 21 ℃ / pH: 5.9 / Method: microdialysis / Details: Krause, K.L., (1987) J.Mol.Biol., 193, 527. | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.8 Å / Num. all: 33922 / Num. obs: 33351 / Redundancy: 6.9 % |
-Processing
Software | Name: X-PLOR / Classification: refinement | ||||||||||||
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Refinement | Resolution: 2.8→8 Å / Rfactor Rwork: 0.18 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 8 Å / Rfactor obs: 0.18 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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