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

Functional role of Asp160 and the deprotonation mechanism of ammonium in the Escherichia coli ammonia channel protein AmtB.

The journal of physical chemistry. B - 9 Apr 2009

Lin Yuchun, Cao Zexing, Mo Yirong

Abstract excerpt

Molecular dynamics simulations on the wild-type AmtB protein and its D160A homology model have been performed. Although no significant structural changes due to the mutation of Asp160 were observed, calculations confirmed the critical role of Asp160 for the recognition and binding of NH(4)(+) in AmtB. The carboxyl group of Asp160 is approximately 8 A from NH(4)(+), but their favorable through-space electrostatic...

Read the complete abstract on PubMed

Topics

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

Share to Aspartic Acid
Share to Cation Transport Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Hydrogen Bonding

Share to Models, Chemical

Share to Protons

Share to Quantum Theory

Share to Quaternary Ammonium Compounds

Source

Open in PubMed Open full text

Identifiers

PMID: 19278252
DOI: 10.1021/jp810651m
PMCID: PMC2676109

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional role of Asp160 and the deprotonation mechanism of ammonium in the Escherichia coli ammonia channel protein AmtB.PMID 19278252Read ↗

Ammonium transport proteins with changes in one of the conserved pore histidines have different performance in ammonia and methylamine conduction.Semantic proximity Read ↗

Substrate binding, deprotonation, and selectivity at the periplasmic entrance of the Escherichia coli ammonia channel AmtB.Semantic proximity Read ↗

The conserved carboxy-terminal region of the ammonia channel AmtB plays a critical role in channel function.Semantic proximity Read ↗

Alternative proton-binding site and long-distance coupling in Escherichia coli sodium-proton antiporter NhaA.Semantic proximity Read ↗

Combined computational and biochemical study reveals the importance of electrostatic interactions between the "pH sensor" and the cation binding site of the sodium/proton antiporter NhaA of Escherichia coli.Semantic proximity Read ↗

An unusual twin-his arrangement in the pore of ammonia channels is essential for substrate conductance.Semantic proximity Read ↗

Effect of Lys84 carbamylation and chloride ion on OXA-143 dynamics and catalytic efficiencySemantic proximity Read ↗

Structural elements in IGP synthase exclude water to optimize ammonia transfer.Semantic proximity Read ↗

Transmembrane segment II of NhaA Na+/H+ antiporter lines the cation passage, and Asp65 is critical for pH activation of the antiporter.Semantic proximity Read ↗

Ammonia-induced formation of an AmtB-GlnK complex is not sufficient for nitrogenase regulation in the photosynthetic bacterium Rhodobacter capsulatus.Semantic proximity Read ↗

Essential role of tyrosine 229 of the oxaloacetate decarboxylase beta-subunit in the energy coupling mechanism of the Na(+) pump.Semantic proximity Read ↗

Computational analysis of ammonia transfer along two intramolecular tunnels in Staphylococcus aureus glutamine-dependent amidotransferase (GatCAB).Semantic proximity Read ↗

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