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Related Concept Videos

ABC Transporters: Exporter01:31

ABC Transporters: Exporter

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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...
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The ADP/ATP Carrier Protein01:42

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ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
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ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

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ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...
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ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

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The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
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ABC Transporters: Importer01:27

ABC Transporters: Importer

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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:
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Updated: Aug 27, 2025

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance SPR
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ATP-Binding Cassette Transporters: Snap-on Complexes?

Iqra Younus1, Sofia Kochkina1, Cheri C Choi1

  • 1Faculty of Biology, Medicine and Health, School of Biological Sciences, The University of Manchester, Manchester, UK.

Sub-Cellular Biochemistry
|September 23, 2022
PubMed
Summary

Assembly of ATP-binding cassette (ABC) transporter complexes, crucial for cellular transport, is explored. This chapter focuses on subunit assembly fidelity and introduces AlphaFold predictions for novel transmembrane domains in bacterial and plant cation exporters.

Keywords:
ABC transportersCo-translational assemblyProtein complexProtein complex assemblyQuaternary structure

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • ATP-binding cassette (ABC) transporters are a large family of membrane proteins vital in prokaryotes.
  • While ABC transporter structures are well-documented, their complex assembly mechanisms remain less understood.
  • These complexes comprise conserved cytoplasmic ATP-binding subunits and diverse transmembrane subunits.

Purpose of the Study:

  • To focus on the assembly processes of ABC transporter complexes.
  • To investigate the fidelity and potential promiscuity in subunit assembly within the cellular environment.
  • To discuss novel findings from the AlphaFold protein structure prediction tool regarding ABC transporter transmembrane domains.

Main Methods:

  • Review of existing literature on ABC transporter structure and function.
  • Analysis of subunit assembly dynamics in prokaryotic organisms.
  • Discussion of predictions generated by the AlphaFold tool for novel transmembrane domain folds.

Main Results:

  • Transmembrane subunits of ABC transporters exhibit significant structural diversity, with seven distinct folds identified.
  • ATP-binding subunits appear to have evolved by attaching to various transmembrane platforms, enabling functional diversity.
  • AlphaFold predicts a new transmembrane domain fold associated with bacterial and plant cation exporters.

Conclusions:

  • The assembly of ABC transporter subunits requires further investigation regarding its fidelity in crowded cellular conditions.
  • Potential promiscuity in the assembly of transmembrane and cytoplasmic components warrants detailed study.
  • Emerging tools like AlphaFold are revealing novel structural insights into ABC transporter families, particularly cation exporters.