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Carrier-Mediated Transport

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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.
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Primary Active Transport

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In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they would not...

Primary Active Transport

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In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps that are embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they...

Primary Active Transport

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Related Experiment Video

Updated: May 26, 2026

Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Functional Characterization of Na⁺/H⁺ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Published on: March 30, 2015

The Na⁺/L-proline transporter PutP.

Heinrich Jung¹, Daniel Hilger, Michael Raba

¹LMU Munich, Biocentre, Microbiology, Grosshaderner Strasse 2-4, Martinsried, D-82152, Germany. hjung@lmu.de

Frontiers in Bioscience (Landmark Edition)

|December 29, 2011

Summary

The Na⁺/L-proline transporter PutP, crucial for nutrient uptake and osmotic stress adaptation in bacteria, has a structure modeled on related symporters. This model, verified experimentally, reveals potential binding sites and transport mechanisms.

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Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles

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Last Updated: May 26, 2026

Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

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Published on: March 30, 2015

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Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles

Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles

Published on: December 31, 2019

Area of Science:

Biochemistry
Structural Biology
Microbiology

Background:

The Na⁺/L-proline transporter PutP is part of the Na⁺/solute symporter family (SLC5).
L-proline uptake is specific to prokaryotic PutP proteins, essential for nutrient utilization and osmotic stress response.
PutP plays a role in bacterial virulence and host interactions.

Purpose of the Study:

To generate a homology model of Escherichia coli PutP.
To elucidate the structural basis of Na⁺ and L-proline binding.
To propose a transport mechanism for PutP.

Main Methods:

Homology modeling based on Vibrio parahaemolyticus Na⁺/galactose symporter crystal structure.
Experimental verification using Cys cross-linking and site-directed spin labeling.
Electron paramagnetic resonance (EPR) spectroscopy.

Main Results:

A homology model of E. coli PutP was constructed, revealing a core structure of transmembrane domains similar to LeuT.
Experimental data validated the homology model.
Putative Na⁺ and L-proline binding sites were identified.

Conclusions:

The study provides a structural model for the Na⁺/L-proline transporter PutP.
The findings offer insights into the transport mechanism and substrate/ion binding.
PutP's structure is crucial for understanding its role in bacterial physiology and pathogenesis.