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

Mutational analysis of the large periplasmic loop 7-8 of the putrescine transporter PotE in Escherichia coli.

The international journal of biochemistry & cell biology - 1 Feb 2004

Minchin Rodney F, McCoubrie Joanne E

Abstract excerpt

The PotE protein is a putrescine-ornithine antiporter found in many gram-negative bacteria. It is a member of the APA family of transporters and has 12 predicted alpha-helical transmembrane spanning segments (TMS). While the substrate binding site has previously been mapped to a region near the surface of the cytoplasmic lipid layer, no structural feature within the periplasmic domains of PotE have been shown to...

Read the complete abstract on PubMed

Topics

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

Share to Oligonucleotides
Share to Antiporters
Share to Glycine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Leucine

Share to Lipid Metabolism

Share to Polyamines

Share to Putrescine

Share to Valine

Source

Identifiers

PMID: 14643892
DOI: 10.1016/s1357-2725(03)00245-0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational analysis of the large periplasmic loop 7-8 of the putrescine transporter PotE in Escherichia coli.PMID 14643892Read ↗

Identification of the putrescine recognition site on polyamine transport protein PotE.Semantic proximity Read ↗

Identification of a glycine motif required for packing in EmrE, a multidrug transporter from Escherichia coli.Semantic proximity Read ↗

Transmembrane domain II of the Na+/proline transporter PutP of Escherichia coli forms part of a conformationally flexible, cytoplasmic exposed aqueous cavity within the membrane.Semantic proximity Read ↗

An amino acid cluster around the essential Glu-14 is part of the substrate- and proton-binding domain of EmrE, a multidrug transporter from Escherichia coli.Semantic proximity Read ↗

Extracellular loop 4 of the proline transporter PutP controls the periplasmic entrance to ligand binding sites.Semantic proximity Read ↗

Functional role of the intracellular loop linking transmembrane domains 6 and 7 of the human dipeptide transporter hPEPT1.Semantic proximity Read ↗

A comparative analysis of single- and multiple-residue substitutions in the alkaline phosphatase signal peptide.Semantic proximity Read ↗

Creation of a fully functional cysteine-less variant of osmosensor and proton-osmoprotectant symporter ProP from Escherichia coli and its application to assess the transporter's membrane orientation.Semantic proximity Read ↗

Evidence for structural symmetry and functional asymmetry in the lactose permease of Escherichia coli.Semantic proximity Read ↗

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

Palmitoylation of POTE family proteins for plasma membrane targeting.Semantic proximity Read ↗

A simple screen for permissive sites in proteins: analysis of Escherichia coli lac permease.Semantic proximity Read ↗

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