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ABC Transporters: Exporter

ABC Transporters: Exporter

ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...

Carrier-Mediated Transport

Carrier-Mediated Transport

Carrier-mediated transport is a pivotal process in drug absorption, particularly for lipid-insoluble drugs, and encompasses facilitated diffusion and active transport. Facilitated diffusion allows drugs to move along their concentration gradient without energy expenditure, while active transport utilizes ATP to drive drug movement against this gradient.
Active transport involves two types of membrane-spanning transporters: uptake and efflux. Uptake transporters are expressed in the small...

Drug Absorption Mechanism: Carrier-Mediated Membrane Transport

Drug Absorption Mechanism: Carrier-Mediated Membrane Transport

Certain large, lipid-insoluble drug molecules that resemble amino acids, peptides, or glucose, require specialized carrier proteins to facilitate their diffusion across cell membranes. This transport can occur through either facilitated diffusion, which does not require energy input, or active transport, which does require energy input.
Facilitated diffusion is a passive process that utilizes human Solute Carrier (SLC) transporters. These transporters bind to the drug, undergo structural...

ABC Transporters: Importer

ABC Transporters: Importer

ATP-binding cassette or ABC transporters are a class of ATP-driven pumps that hydrolyze ATP to move solutes across the membrane. They can be grouped into importers and exporters. While exporters are present in all domains of life, importers exist only in bacteria and some plants.
In bacteria, based on the number of transmembrane helices and the chemical nature of their substrates, the ABC importers can be divided into three types:

Membrane Transporters

Membrane Transporters

Transporters are essential membrane transport proteins with functions related to cell nutrition, homeostasis, communication, etc. Approximately 7% of all genes in the human genome code for transporters or transporter-related proteins.
Transporters are mainly composed of alpha-helices, built from bundles of ten or more helices traversing the plasma membrane. The solute-binding sites are located midway, where some of the helices are broken or distorted, making space for the binding site through...

Facilitated Diffusion

Facilitated Diffusion

The plasma membrane, a critical structure in cellular biology, houses an array of transporters, or carrier proteins, interspersed within its lipid bilayer. These proteins play a crucial role in solute transport through facilitated diffusion, a form of passive diffusion that uses transporters to move the molecules across the membrane.
In this process, substrates such as organic compounds and ions interact with a transporter on one side, triggering conformational changes in proteins that enable...

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Related Experiment Video

Updated: Jul 15, 2026

Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein

Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein

Published on: December 3, 2010

E. coli multidrug transporter MdfA is a monomer.

Nadejda Sigal¹, Oded Lewinson, Sharon G Wolf

¹Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.

|April 5, 2007

Summary

The multidrug transporter MdfA from E. coli functions as an active monomer. This research clarifies MdfA

Area of Science:

Molecular Biology
Biochemistry
Structural Biology

Background:

MdfA is a secondary multidrug transporter found in E. coli.
It confers resistance to various toxic compounds through active export.
Understanding MdfA's structure and function is crucial for elucidating drug transport mechanisms.

Purpose of the Study:

To investigate the biochemical properties and structural characteristics of MdfA.
To prepare MdfA for high-resolution structural studies.
To understand the mechanism of substrate recognition and translocation.

Main Methods:

Purification of MdfA using 6-His tag, metal affinity chromatography, and size exclusion chromatography (SE-HPLC).
Analysis of purified MdfA for beta-dodecyl maltopyranoside (DDM) and phospholipid (PL) content.

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Assay of tetraphenylphosphonium (TPP+) binding activity.

Electron crystallography and 3D reconstruction of two-dimensional crystals.

Main Results:

Purified MdfA was found to be active in DDM solution.
Analysis indicated MdfA is monomeric in DDM solution.
Electron crystallography data suggest MdfA is also monomeric in reconstituted proteoliposomes.

Conclusions:

MdfA functions as an active monomer in detergent solution.
The findings support a monomeric state for MdfA within proteoliposomes.
This study provides essential biochemical and structural insights into MdfA's function.