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-A resolution
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A database of macromolecular motionsAllosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutaseReplacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylaseAssessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunitFrom Genome to Structure and Back Again: A Family Portrait of the TranscarbamylasesBinding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulationStructure of the catalytic trimer ofMethanococcus jannaschiiaspartate transcarbamoylase in an orthorhombic crystal formMolecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolutionMetal Ion Involvement in the Allosteric Mechanism of Escherichia coli Aspartate TranscarbamoylaseA Second Allosteric Site in Escherichia coli Aspartate TranscarbamoylaseStructure of the catalytic chain ofMethanococcus jannaschiiaspartate transcarbamoylase in a hexagonal crystal form: insights into the path of carbamoyl phosphate to the active site of the enzymeStructure and mechanisms of Escherichia coli aspartate transcarbamoylaseTime Evolution of the Quaternary Structure of Escherichia coli Aspartate Transcarbamoylase upon Reaction with the Natural Substrates and a Slow, Tight-Binding InhibitorX-ray Scattering Studies of Protein Structural Dynamics.The structural basis of ATP as an allosteric modulatorAsymmetric allosteric signaling in aspartate transcarbamoylase.A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transitionOptimized torsion-angle normal modes reproduce conformational changes more accurately than cartesian modes.Allostery and cooperativity in Escherichia coli aspartate transcarbamoylaseWeakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylaseThe use of nucleotide analogs to evaluate the mechanism of the heterotropic response of Escherichia coli aspartate transcarbamoylase.Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: genetic organization, structure, and expression in Escherichia coli.A molecular mechanism for pyrimidine and purine nucleotide control of aspartate transcarbamoylase.Strain analysis of protein structures and low dimensionality of mechanical allosteric couplings.1H NMR studies on the catalytic subunit of aspartate transcarbamoylase.Heterotropic interactions in aspartate transcarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation.ASD v2.0: updated content and novel features focusing on allosteric regulation.Aspartate carbamoyltransferase from the thermoacidophilic archaeon Sulfolobus acidocaldarius. Cloning, sequence analysis, enzyme purification and characterization.Temperature effects on the allosteric responses of native and chimeric aspartate transcarbamoylases.Conversion of the allosteric regulatory patterns of aspartate transcarbamoylase by exchange of a single beta-strand between diverged regulatory chains.A study into the effects of protein binding on nucleotide conformationExpression, purification, crystallization and preliminary X-ray crystallographic studies of a cold-adapted aspartate carbamoyltransferase from Moritella profunda.Aspartate-90 and arginine-269 of hamster aspartate transcarbamylase affect the oligomeric state of a chimaeric protein with an Escherichia coli maltose-binding domain.Aquifex aeolicus aspartate transcarbamoylase, an enzyme specialized for the efficient utilization of unstable carbamoyl phosphate at elevated temperature.Stabilization of the R allosteric structure of Escherichia coli aspartate transcarbamoylase by disulfide bond formation.A fluorescent probe-labeled Escherichia coli aspartate transcarbamoylase that monitors the allosteric conformational state.240s loop interactions stabilize the T state of Escherichia coli aspartate transcarbamoylase.Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.Aspartate Transcarbamylase from Escherichia Coli: Activity and Regulation
P2860
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P2860
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-A resolution
description
1990 nî lūn-bûn
@nan
1990 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Structural consequences of eff ...... ed enzymes at 2.6-A resolution
@ast
Structural consequences of eff ...... ed enzymes at 2.6-A resolution
@en
Structural consequences of eff ...... ed enzymes at 2.6-A resolution
@nl
type
label
Structural consequences of eff ...... ed enzymes at 2.6-A resolution
@ast
Structural consequences of eff ...... ed enzymes at 2.6-A resolution
@en
Structural consequences of eff ...... ed enzymes at 2.6-A resolution
@nl
prefLabel
Structural consequences of eff ...... ed enzymes at 2.6-A resolution
@ast
Structural consequences of eff ...... ed enzymes at 2.6-A resolution
@en
Structural consequences of eff ...... ed enzymes at 2.6-A resolution
@nl
P2093
P356
P1433
P1476
Structural consequences of eff ...... ed enzymes at 2.6-A resolution
@en
P2093
J E Gouaux
R C Stevens
W N Lipscomb
P304
P356
10.1021/BI00485A019
P407
P577
1990-08-21T00:00:00Z