A Single Amino Acid Substitution in the Active Site of Escherichia coli Aspartate Transcarbamoylase Prevents the Allosteric Transition

Modeling of the tetrahedral intermediate within the active site of Escherichia coli aspartate transcarbamoylase revealed a specific interaction with the side-chain of Gln137, an interaction not previously observed in the structure of the X-ray enzyme in the presence of N-phosphonacetyl- l-aspartate...

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Veröffentlicht in:	Journal of molecular biology 2005-06, Vol.349 (2), p.413-423
Hauptverfasser:	Stieglitz, Kimberly A., Pastra-Landis, Styliani C., Xia, Jiarong, Tsuruta, Hiro, Kantrowitz, Evan R.
Format:	Artikel
Sprache:	eng
Schlagworte:	allosteric enzyme Allosteric Regulation Amino Acid Substitution - genetics Aspartate Carbamoyltransferase - chemistry Aspartate Carbamoyltransferase - genetics Aspartate Carbamoyltransferase - metabolism Aspartic Acid - analogs & derivatives Aspartic Acid - metabolism Binding Sites Crystallography, X-Ray electrostatics Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Glutamine - genetics Glutamine - metabolism Models, Molecular Phosphonoacetic Acid - analogs & derivatives Phosphonoacetic Acid - metabolism Poisson–Boltzmann equation polar contacts Protein Structure, Quaternary Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism small-angle X-ray scattering Static Electricity Structure-Activity Relationship
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