Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The role of intersubunit interactions for the stabilization of the T state of Escherichia coli aspartate transcarbamoylase.

The Journal of biological chemistry - 20 Dec 2002

Chan Robin S, Sakash Jessica B, Macol Christine P, West Jay M, Tsuruta Hiro, Kantrowitz Evan R

Abstract excerpt

Homotropic cooperativity in Escherichia coli aspartate transcarbamoylase results from the substrate-induced transition from the T to the R state. These two alternate states are stabilized by a series of interdomain and intersubunit interactions. The salt link between Lys-143 of the regulatory chain and Asp-236 of the catalytic chain is only observed in the T state. When Asp-236 is replaced by alanine the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alanine
Share to Allosteric Site

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Aspartate Carbamoyltransferase

Share to Aspartic Acid

Share to Chromatography, Ion Exchange

Share to Phosphonoacetic Acid

Share to Scattering, Radiation

Share to X-Rays

Source

Identifiers

PMID: 12399459
DOI: 10.1074/jbc.M208919200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The role of intersubunit interactions for the stabilization of the T state of Escherichia coli aspartate transcarbamoylase.PMID 12399459Read ↗

Stabilization of the R allosteric structure of Escherichia coli aspartate transcarbamoylase by disulfide bond formation.Semantic proximity Read ↗

Importance of domain closure for the catalysis and regulation of Escherichia coli aspartate transcarbamoylase.Semantic proximity Read ↗

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.Semantic proximity Read ↗

Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylase.Semantic proximity Read ↗

Monitoring the transition from the T to the R state in E.coli aspartate transcarbamoylase by X-ray crystallography: crystal structures of the E50A mutant enzyme in four distinct allosteric states.Semantic proximity Read ↗

Structure of the E.coli aspartate transcarbamoylase trapped in the middle of the catalytic cycle.Semantic proximity Read ↗

Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.Semantic proximity Read ↗

Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase.Semantic proximity Read ↗

Function of serine-171 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamoylase.Semantic proximity Read ↗

Long range effects of amino acid substitutions in the catalytic chain of aspartate transcarbamoylase. Localized replacements in the carboxyl-terminal alpha-helix cause marked alterations in allosteric properties and intersubunit interactions.Semantic proximity Read ↗

Modelling allosteric processes in E coli aspartate transcarbamylase.Semantic proximity Read ↗

Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.