CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL P*H

RESIDUES PRO A 268 AND PRO C 268 ARE CIS-PROLINES.

Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-A resolution and neutral pH.

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

Crystal Structures of Aspartate Carbamoyltransferase Ligated with Phosphonoacetamide, Malonate, and Ctp or ATP at 2.8-Angstroms Resolution and Neutral Ph

Structure of a Single Amino Acid Mutant of Aspartate Carbamoyltransferase at 2.5-Angstroms Resolution. Implications for the Cooperative Mechanism

Structural Transitions in Crystals of Native Aspartate Carbamoyltransferase

Complex of N-Phosphonacetyl-L-Aspartate with Aspartate Carbamoyltransferase. X-Ray Refinement, Analysis of Conformational Changes and Catalytic and Allosteric Mechanisms

Escherichia Coli Aspartate Transcarbamylase. The Relation between Structure and Function

Three-Dimensional Structure of Carbamoyl Phosphate and Succinate Bound to Aspartate Carbamoyltransferase

Structural Asymmetry in the Ctp-Liganded Form of Aspartate Carbamoyltransferase from Escherichia Coli

2.5 Angstroms Structure of Aspartate Carbamoyltransferase Complexed with the Bisubstrate Analog N-(Phosphonacetyl)-L-Aspartate

The Catalytic Mechanism of Escherichia Coli Aspartate Carbamoyltransferase. A Molecular Modelling Study

Structure at 2.9-Angstroms Resolution of Aspartate Carbamoyltransferase Complexed with the Bisubstrate Analogue N-(Phosphonacetyl)-L-Aspartate

Structure of Unligated Aspartate Carbamoyltransferase of Escherichia Coli at 2.6-Angstroms Resolution

Crystal and Molecular Structures of Native and Ctp-Liganded Aspartate Carbamoyltransferase from Escherichia Coli

Interactions of Phosphate Ligands with Escherichia Coli Aspartate Carbamoyltransferase in the Crystalline State

Interactions of Metal-Nucleotide Complexes with Aspartate Carbamoyltransferase in the Crystalline State

Gross Quaternary Changes in Aspartate Carbamoyltransferase are Induced by the Binding of N-(Phosphonacetyl)-L-Aspartate. A 3.5-Angstroms Resolution Study

A 3.0-Angstroms Resolution Study of Nucleotide Complexes with Aspartate Carbamoyltransferase

Three-Dimensional Structures of Aspartate Carbamoyltransferase from Escherichia Coli and of its Complex with Cytidine Triphosphate

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
Binding Site at 5.5 Angstroms Resolution of Cytidine Triphosphate, the Allosteric Inhibitor of Aspartate Transcarbamylase from Escherichia Coli. Relation to Mechanisms of Control

Aspartate Transcarbamoylase from Escherichia Coli. Electron Density at 5.5 Angstroms Resolution

ASPARTATE CARBAMOYLTRANSFERASE, CATALYTIC CHAIN

ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN

ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCARBAMYLASE) (R STATE) (E.C.2.1.3.2) COMPLEX WITH PHOSPHONOACETAMIDE (PAM) AND MALONATE (MLI)

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.

BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS A

BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS C