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

OprG Harnesses the Dynamics of its Extracellular Loops to Transport Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa.

Structure (London, England : 1993) - 1 Dec 2015

Kucharska Iga, Seelheim Patrick, Edrington Thomas, Liang Binyong, Tamm Lukas K

Abstract excerpt

OprG is an outer membrane protein of Pseudomonas aeruginosa whose function as an antibiotic-sensitive porin has been controversial and not well defined. Circumstantial evidence led to the proposal that OprG might transport hydrophobic compounds by using a lateral gate in the barrel wall thought to be lined by three conserved prolines. To test this hypothesis and to find the physiological substrates of OprG, we...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Amino Acids

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

Share to Bacterial Outer Membrane Proteins

Share to Conserved Sequence

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Binding

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 26655471
DOI: 10.1016/j.str.2015.10.009
PMCID: PMC4699568

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

OprG Harnesses the Dynamics of its Extracellular Loops to Transport Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa.PMID 26655471Read ↗

Toward Understanding the Outer Membrane Uptake of Small Molecules by Pseudomonas aeruginosaSemantic proximity Read ↗

Structure, Dynamics, and Substrate Specificity of the OprO Porin from Pseudomonas aeruginosa.Semantic proximity Read ↗

Opening the pore hinges on proline.Semantic proximity Read ↗

Local structural constraints and charge distribution in the protegrin-1 arginine loop govern activity against colistin-resistant Klebsiella pneumoniae.Semantic proximity Read ↗

Investigating the mode of action of proline-rich antimicrobial peptides using a genetic approach: a tool to identify new bacterial targets amenable to the design of novel antibiotics.Semantic proximity Read ↗

How to Enter a Bacterium: Bacterial Porins and the Permeation of AntibioticsSemantic proximity Read ↗

Relocation of active site carboxylates in major facilitator superfamily multidrug transporter LmrP reveals plasticity in proton interactions.Semantic proximity Read ↗

Substrate Specificity within a Family of Outer Membrane Carboxylate ChannelsSemantic proximity Read ↗

In vivo analysis reveals substrate-gating mutants of a rhomboid intramembrane protease display increased activity in living cells.Semantic proximity Read ↗

Role of the central arginine R133 toward the ion selectivity of the phosphate specific channel OprP: effects of charge and solvation.Semantic proximity Read ↗

Hydrophilicity of a single residue within MscL correlates with increased channel mechanosensitivity.Semantic proximity Read ↗

Pivotal role of the glycine-rich TM3 helix in gating the MscS mechanosensitive channel.Semantic proximity Read ↗

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