Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferase. X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms
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In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assemblyRandom circular permutation leading to chain disruption within and near alpha helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability, and functionStructural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase.Replacement 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 subunitIntegrated allosteric regulation in the S. cerevisiae carbamylphosphate synthetase - aspartate transcarbamylase multifunctional proteinFrom 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 regulationHuman ornithine transcarbamylase: crystallographic insights into substrate recognition and conformational changesThe conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroniArginine 54 in the active site of escherichia coli aspartate transcarbamoylase is critical for catalysis: A site-specific mutagenesis, NMR, and X-ray crystallographic studyA single mutation in the active site swaps the substrate specificity ofN-acetyl-L-ornithine transcarbamylase andN-succinyl-L-ornithine transcarbamylaseThe first high pH structure ofEscherichia coliaspartate transcarbamoylaseStructure of the catalytic trimer ofMethanococcus jannaschiiaspartate transcarbamoylase in an orthorhombic crystal formThe Pathway of Product Release from the R State of 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 transcarbamoylaseCrystal structure of Pseudomonas aeruginosa catabolic ornithine transcarbamoylase at 3.0-A resolution: a different oligomeric organization in the transcarbamoylase familySubstrate-induced conformational change in a trimeric ornithine 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.Crystal structure of the Glu-239----Gln mutant of aspartate carbamoyltransferase at 3.1-A resolution: an intermediate quaternary structure.Mammalian aspartate transcarbamylase (ATCase): sequence of the ATCase domain and interdomain linker in the CAD multifunctional polypeptide and properties of the isolated domain.A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transitionDirect observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase.Optimized torsion-angle normal modes reproduce conformational changes more accurately than cartesian modes.Allostery and cooperativity in Escherichia coli aspartate transcarbamoylasePeptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase.In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains.Molecular dynamics simulations and rigid body (TLS) analysis of aspartate carbamoyltransferase: evidence for an uncoupled R stateReconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chainsGlu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure.Association of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability.Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylaseThe allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closureStructural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: implications for domain switching.Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase.In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chainsAspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: genetic organization, structure, and expression in Escherichia coli.
P2860
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P2860
Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferase. X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms
description
1988 nî lūn-bûn
@nan
1988 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年学术文章
@wuu
1988年学术文章
@zh-cn
1988年学术文章
@zh-hans
1988年学术文章
@zh-my
1988年学术文章
@zh-sg
1988年學術文章
@yue
name
Complex of N-phosphonacetyl-L- ...... ytic and allosteric mechanisms
@ast
Complex of N-phosphonacetyl-L- ...... ytic and allosteric mechanisms
@en
Complex of N-phosphonacetyl-L- ...... ytic and allosteric mechanisms
@nl
type
label
Complex of N-phosphonacetyl-L- ...... ytic and allosteric mechanisms
@ast
Complex of N-phosphonacetyl-L- ...... ytic and allosteric mechanisms
@en
Complex of N-phosphonacetyl-L- ...... ytic and allosteric mechanisms
@nl
prefLabel
Complex of N-phosphonacetyl-L- ...... ytic and allosteric mechanisms
@ast
Complex of N-phosphonacetyl-L- ...... ytic and allosteric mechanisms
@en
Complex of N-phosphonacetyl-L- ...... ytic and allosteric mechanisms
@nl
P2093
P1476
Complex of N-phosphonacetyl-L- ...... ytic and allosteric mechanisms
@en
P2093
P304
P407
P577
1988-12-05T00:00:00Z