Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity
about
Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase.From Genome to Structure and Back Again: A Family Portrait of the TranscarbamylasesThe binding of inosine monophosphate to Escherichia coli carbamoyl phosphate synthetaseThe Pathway of Product Release from the R State of Aspartate TranscarbamoylaseA Cooperative Escherichia coli Aspartate Transcarbamoylase without Regulatory Subunits,Metal Ion Involvement in the Allosteric Mechanism of Escherichia coli Aspartate TranscarbamoylaseStructure and mechanisms of Escherichia coli aspartate transcarbamoylase1.85-A resolution crystal structure of human ornithine transcarbamoylase complexed with N-phosphonacetyl-L-ornithine. Catalytic mechanism and correlation with inherited deficiencyThe molecular basis of ornithine transcarbamylase deficiency: modelling the human enzyme and the effects of mutationsAllostery 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.Submicromolar phosphinic inhibitors of Escherichia coli aspartate transcarbamoylase.Synthesis and in vitro evaluation of aspartate transcarbamoylase inhibitors.Artificial allosteric receptors.From feedback inhibition to allostery: the enduring example of aspartate transcarbamoylase.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.240s loop interactions stabilize the T state of Escherichia coli aspartate transcarbamoylase.Aspartate Transcarbamylase from Escherichia Coli: Activity and Regulation
P2860
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P2860
Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity
description
1993 nî lūn-bûn
@nan
1993 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Crystal structure of CTP-ligat ...... nism of negative cooperativity
@ast
Crystal structure of CTP-ligat ...... nism of negative cooperativity
@en
Crystal structure of CTP-ligat ...... nism of negative cooperativity
@nl
type
label
Crystal structure of CTP-ligat ...... nism of negative cooperativity
@ast
Crystal structure of CTP-ligat ...... nism of negative cooperativity
@en
Crystal structure of CTP-ligat ...... nism of negative cooperativity
@nl
prefLabel
Crystal structure of CTP-ligat ...... nism of negative cooperativity
@ast
Crystal structure of CTP-ligat ...... nism of negative cooperativity
@en
Crystal structure of CTP-ligat ...... nism of negative cooperativity
@nl
P2093
P356
P1433
P1476
Crystal structure of CTP-ligat ...... nism of negative cooperativity
@en
P2093
J E Gouaux
R P Kosman
W N Lipscomb
P304
P356
10.1002/PROT.340150206
P407
P577
1993-02-01T00:00:00Z