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

Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance.

Structure (London, England : 1993) - 1 Jun 2005

Gatzeva-Topalova Petia Z, May Andrew P, Sousa Marcelo C

Abstract excerpt

The modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) allows gram-negative bacteria to resist the antimicrobial activity of cationic antimicrobial peptides and antibiotics such as polymyxin. ArnA is the first enzyme specific to the lipid A-Ara4N pathway. It contains two functionally and physically separable domains: a dehydrogenase domain (ArnA_DH) catalyzing the NAD+-dependent oxidative...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Catalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Drug Resistance, Microbial

Share to Hydrogen Bonding

Share to Hydroxymethyl and Formyl Transferases

Share to Molecular Conformation

Share to Spectrum Analysis, Raman

Source

Open in PubMed Open full text

Identifiers

PMID: 15939024
DOI: 10.1016/j.str.2005.03.018
PMCID: PMC2997725

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

Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance.PMID 15939024Read ↗

Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis.Semantic proximity Read ↗

Structural basis for substrate specificity in ArnB. A key enzyme in the polymyxin resistance pathway of Gram-negative bacteria.Semantic proximity Read ↗

Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose.Semantic proximity Read ↗

Burkholderia cenocepacia and Salmonella enterica ArnT proteins that transfer 4-amino-4-deoxy-l-arabinose to lipopolysaccharide share membrane topology and functional amino acids.Semantic proximity Read ↗

Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation.Semantic proximity Read ↗

An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor.Semantic proximity Read ↗

A structural perspective on the enzymes that convert dTDP-d-glucose into dTDP-l-rhamnoseSemantic proximity Read ↗

A survey of ADP-ribosyltransferase families in the pathogenic <i>Legionella</i>Semantic proximity Read ↗

A Legionella effector ADP-ribosyltransferase inactivates glutamate dehydrogenaseSemantic proximity Read ↗

Inactivation of the arn operon and loss of aminoarabinose on lipopolysaccharide as the cause of susceptibility to colistin in an atypical clinical isolate of proteus vulgaris.Semantic proximity Read ↗

A <i>Legionella</i> effector ADP-ribosyltransferase inactivates glutamate dehydrogenaseSemantic proximity Read ↗

UDP-hexose 4-epimerases: a view on structure, mechanism and substrate specificity.Semantic proximity Read ↗

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