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Related Concept Videos

ABC Transporters: Exporter01:31

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...
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
ABC Transporters: Importer01:27

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:
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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Related Experiment Video

Updated: Jun 13, 2026

ABCG5/G8 Crystallization in a Lipidic Bicelle Environment for X-Ray Crystallography
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Asymmetric switching in a homodimeric ABC transporter: a simulation study.

Jussi Aittoniemi1, Heidi de Wet, Frances M Ashcroft

  • 1Department of Biochemistry, University of Oxford, Oxford, United Kingdom.

Plos Computational Biology
|May 11, 2010
PubMed
Summary

This study reveals how symmetric ABC transporters achieve asymmetric ATP hydrolysis, crucial for their function. Molecular dynamics simulations show transient asymmetry in nucleotide-binding sites, explaining sequential hydrolysis in both bacterial and eukaryotic transporters.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Dynamics

Background:

  • ABC transporters are vital membrane proteins regulating cellular processes like drug resistance.
  • Understanding their nucleotide-binding sites (NBSs) is key, as ATP hydrolysis is cooperative and non-simultaneous.
  • The mechanism of sequential ATP hydrolysis in symmetric transporters remains unclear.

Purpose of the Study:

  • To elucidate the mechanism of sequential ATP hydrolysis in symmetric ABC transporters.
  • To investigate how initial symmetry transitions to asymmetry at the NBSs.
  • To extend findings to eukaryotic ABC exporters with non-identical NBSs.

Main Methods:

  • Molecular dynamics simulations of the homodimeric multidrug exporter Sav1866.
  • Analysis of nucleotide-binding site (NBS) transitions and residue interactions.
  • Comparison of bacterial Sav1866 mechanisms with eukaryotic ABC transporter structures.

Main Results:

  • Symmetric Sav1866 structures exhibit asymmetric NBS transitions in pre-hydrolytic states.
  • Molecular switches involving MgATP-binding and charged residues facilitate sequential hydrolysis.
  • Degenerate NBSs in eukaryotic transporters mirror asymmetric switching residues found in Sav1866.

Conclusions:

  • Asymmetric conformational switching at NBSs is inherent in symmetric ABC transporters.
  • This mechanism explains sequential ATP hydrolysis, essential for transporter function.
  • Findings suggest degenerate NBSs in eukaryotic ABCs pre-determine hydrolysis sequence, aligning with bacterial mechanisms.