Related Experiment Video
Updated: Aug 3, 2026

Mapping Bacterial Functional Networks and Pathways in Escherichia Coli using Synthetic Genetic Arrays
Published on: November 12, 2012
Bipartite gating in the outer membrane protein FecA
D van der Helm1, R Chakraborty, A D Ferguson
1Department of Chemistry and Biochemistry, University of Oklahoma, 620 Parrington Oval, Norman, OK 73019, USA. dvdhelm@chemdept.chem.ou.edu
The FecA protein utilizes a two-gate system for transport, distinguishing between ligand binding and the actual transport process. This bipartite gating mechanism provides new insights into protein transport systems.
Area of Science:
- Structural Biology
- Biochemistry
- Molecular Biology
Background:
- FecA is a key transporter protein involved in iron uptake.
- Understanding the transport mechanism of FecA is crucial for deciphering cellular nutrient acquisition.
Purpose of the Study:
- To elucidate the structural basis of FecA's transport mechanism.
- To investigate the role of distinct structural elements in ligand binding and translocation.
Main Methods:
- X-ray crystallography was used to determine the structure of FecA.
- Comparative structural analysis of FecA with and without bound ligand.
Main Results:
- The structure determination revealed two distinct gating mechanisms within FecA.
- Extracellular loops form a gate over the ligand-binding site.
- An internal plug controls passage through the barrel structure.
Conclusions:
- FecA employs a bipartite gating system for transport.
- This mechanism allows for a clear separation between ligand binding and transport events.
- Provides a framework for understanding related transporter proteins.
More Related Videos
10:24Separation of the Cell Envelope for Gram-negative Bacteria into Inner and Outer Membrane Fractions with Technical Adjustments for Acinetobacter baumannii
Published on: April 10, 2020
08:38Application of Flow Vermimetry for Quantification and Analysis of the Caenorhabditis elegans Gut Microbiome
Published on: March 31, 2023
Related Concept Videos
Insertion of Multi-pass Transmembrane Proteins in the RER
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
GPI Anchoring of Proteins in the ER Membrane
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
Multi-pass Transmembrane Proteins and β-barrels
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
GPCRs Regulate Adenylyl Cylase Activity
Two...
Bacterial Gastroenteritis
Amebiasis