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- PDB-3at1: CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOA... -
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Basic information
Entry | Database: PDB / ID: 3at1 | ||||||
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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 | ||||||
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![]() | TRANSFERASE (CARBAMOYL-P / ASPARTATE) | ||||||
Function / homology | ![]() 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 / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Gouaux, J.E. / Lipscomb, W.N. | ||||||
![]() | ![]() Title: Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-A resolution and neutral pH. Authors: Gouaux, J.E. / Lipscomb, W.N. #1: ![]() 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: ![]() 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: ![]() 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. #4: ![]() Title: Structural Transitions in Crystals of Native Aspartate Carbamoyltransferase Authors: Gouaux, J.E. / Lipscomb, W.N. #5: ![]() Title: Complex of N-Phosphonacetyl-L-Aspartate with Aspartate Carbamoyltransferase. X-Ray Refinement, Analysis of Conformational Changes and Catalytic and Allosteric Mechanisms Authors: Ke, H. / Lipscomb, W.N. / Cho, Y. / Honzatko, R.B. #6: ![]() Title: Escherichia Coli Aspartate Transcarbamylase. The Relation between Structure and Function Authors: Kantrowitz, E.R. / Lipscomb, W.N. #7: ![]() Title: Three-Dimensional Structure of Carbamoyl Phosphate and Succinate Bound to Aspartate Carbamoyltransferase Authors: Gouaux, J.E. / Lipscomb, W.N. #8: ![]() 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: ![]() 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: ![]() Title: The Catalytic Mechanism of Escherichia Coli Aspartate Carbamoyltransferase. A Molecular Modelling Study Authors: Gouaux, J.E. / Krause, K.L. / Lipscomb, W.N. #11: ![]() 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: ![]() Title: Structure of Unligated Aspartate Carbamoyltransferase of Escherichia Coli at 2.6-Angstroms Resolution Authors: Ke, H. / Honzatko, R.B. / Lipscomb, W.N. #13: ![]() 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: ![]() Title: Interactions of Phosphate Ligands with Escherichia Coli Aspartate Carbamoyltransferase in the Crystalline State Authors: Honzatko, R.B. / Lipscomb, W.N. #15: ![]() Title: Interactions of Metal-Nucleotide Complexes with Aspartate Carbamoyltransferase in the Crystalline State Authors: Honzatko, R.B. / Lipscomb, W.N. #16: ![]() 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: ![]() Title: A 3.0-Angstroms Resolution Study of Nucleotide Complexes with Aspartate Carbamoyltransferase Authors: Honzatko, R.B. / Monaco, H.L. / Lipscomb, W.N. #18: ![]() 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: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 184.5 KB | Display | ![]() |
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PDB format | ![]() | 147.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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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: (-0.255348, -0.966776, 0.011879), Vector: Details | THE ENZYME IS A DODECAMER COMPOSED OF SIX CATALYTIC CHAINS AND SIX REGULATORY CHAINS THAT CAN BE DISSOCIATED INTO SUBUNITS. THE ASYMMETRIC UNIT OF THE CRYSTAL CONSISTS OF ONE THIRD OF THE MOLECULE - TWO CATALYTIC AND TWO REGULATORY CHAINS. CHAINS *A* AND *C* (REFERRED TO AS C1 AND C6 RESPECTIVELY IN THE *JRNL* REFERENCE ABOVE) ARE THE CATALYTIC CHAINS CONSISTING OF 310 RESIDUES EACH. CHAINS *B* AND *D* (REFERRED TO AS R1 AND R6 RESPECTIVELY IN THE *JRNL* REFERENCE ABOVE) ARE THE REGULATORY CHAINS CONSISTING OF 153 RESIDUES EACH. 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. | |
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Components
#1: Protein | Mass: 34337.105 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | Mass: 17072.549 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Chemical | #4: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.99 Å3/Da / Density % sol: 58.86 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5.8 / Method: microdialysisDetails: referred to Proc.Nat.Acad.Sci.,U.S.A.86.845-848 1989 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 6 Å / Num. obs: 22745 / % possible obs: 87 % / Num. measured all: 73039 / Rmerge(I) obs: 0.079 |
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Processing
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Refinement | Resolution: 2.8→6 Å / Rfactor Rwork: 0.181 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→6 Å
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Refine LS restraints |
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Refinement | *PLUS Num. reflection obs: 19708 / Highest resolution: 2.8 Å / Lowest resolution: 8 Å / Rfactor obs: 0.181 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d |