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

Lipopolysaccharide binding to the periplasmic protein LptA.

Protein science : a publication of the Protein Society - 1 Aug 2017

Schultz Kathryn M, Lundquist Tanner J, Klug Candice S

Abstract excerpt

Lipopolysaccharide (LPS) and the periplasmic protein, LptA, are two essential components of Gram-negative bacteria. LPS, also known as endotoxin, is found asymmetrically distributed in the outer leaflet of the outer membrane of Gram-negative bacteria such as Escherichia coli and plays a role in the organism's natural defense in adverse environmental conditions. LptA is a member of the lipopolysaccharide transport...

Read the complete abstract on PubMed

Topics

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

Share to Electron Spin Resonance Spectroscopy
Share to Lipopolysaccharides

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

Share to Periplasm

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protein Interaction Domains and Motifs

Share to Protein Multimerization

Share to Spin Labels

Source

Open in PubMed Open full text

Identifiers

PMID: 28419595
DOI: 10.1002/pro.3177
PMCID: PMC5521551

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

Lipopolysaccharide binding to the periplasmic protein LptA.PMID 28419595Read ↗

Characterization of and lipopolysaccharide binding to the E. coli LptC protein dimer.Semantic proximity Read ↗

An induced folding process characterizes the partial-loss of function mutant LptAI36D in its interactions with ligands.Semantic proximity Read ↗

The Escherichia coli Lpt transenvelope protein complex for lipopolysaccharide export is assembled via conserved structurally homologous domains.Semantic proximity Read ↗

The Lack of the Essential LptC Protein in the Trans-Envelope Lipopolysaccharide Transport Machine Is Circumvented by Suppressor Mutations in LptF, an Inner Membrane Component of the Escherichia coli Transporter.Semantic proximity Read ↗

Periplasmic orientation of nascent lipid A in the inner membrane of an Escherichia coli LptA mutant.Semantic proximity Read ↗

Cytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. coli.Semantic proximity Read ↗

Genetic analysis reveals a robust and hierarchical recruitment of the LolA chaperone to the LolCDE lipoprotein transporterSemantic proximity Read ↗

NMR identification of the binding surfaces involved in the Salmonella and Shigella Type III secretion tip-translocon protein-protein interactions.Semantic proximity Read ↗

Structural investigation of the interaction between LolA and LolB using NMR.Semantic proximity Read ↗

Mutational analysis of the essential lipopolysaccharide-transport protein LptH of Pseudomonas aeruginosa to uncover critical oligomerization sites.Semantic proximity Read ↗

Small siphophage binding to an open state of the LptDE outer membrane lipopolysaccharide transloconSemantic proximity Read ↗

BamA β16C strand and periplasmic turns are critical for outer membrane protein insertion and assembly.Semantic proximity Read ↗

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