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ASPARTATE TRANSCARBAMOYLASE REGULATORY CHAIN MUTANT (T82A)
Descriptor:	ASPARTATE TRANSCARBAMOYLASE, D-MALATE, ZINC ION
Authors:	Williams, M.K, Stec, B, Kantrowitz, E.R.
Deposit date:	1998-04-25
Release date:	1998-10-14
Last modified:	2023-08-09
Method:	X-RAY DIFFRACTION (2.6 Å)
Cite:	A single mutation in the regulatory chain of Escherichia coli aspartate transcarbamoylase results in an extreme T-state structure. J.Mol.Biol., 281, 1998

Structure of a regulatory subunit mutant D19A of ATCase from E. coli
Descriptor:	Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, ZINC ION
Authors:	Stec, B, Williams, M.K, Stieglitz, K.A, Kantrowitz, E.R.
Deposit date:	2007-06-28
Release date:	2008-02-19
Last modified:	2024-02-21
Method:	X-RAY DIFFRACTION (2.7 Å)
Cite:	Comparison of two T-state structures of regulatory-chain mutants of Escherichia coli aspartate transcarbamoylase suggests that His20 and Asp19 modulate the response to heterotropic effectors. Acta Crystallogr.,Sect.D, 63, 2007

Structure of regulatory chain mutant H20A of asparate transcarbamoylase from E. coli
Descriptor:	Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, ZINC ION
Authors:	Stec, B, Williams, M.K, Stieglitz, K.A, Kantrowitz, E.R.
Deposit date:	2007-06-28
Release date:	2008-02-19
Last modified:	2023-08-30
Method:	X-RAY DIFFRACTION (2.2 Å)
Cite:	Comparison of two T-state structures of regulatory-chain mutants of Escherichia coli aspartate transcarbamoylase suggests that His20 and Asp19 modulate the response to heterotropic effectors. Acta Crystallogr.,Sect.D, 63, 2007

Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-carbamyl-L-aspartate Ligated Enzyme
Descriptor:	Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, N-CARBAMOYL-L-ASPARTATE, ...
Authors:	Huang, J, Lipscomb, W.N.
Deposit date:	2003-09-19
Release date:	2004-06-08
Last modified:	2023-08-23
Method:	X-RAY DIFFRACTION (2.37 Å)
Cite:	Products in the T-State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-Carbamyl-l-aspartate Ligated Enzyme Biochemistry, 43, 2004