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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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ABC Transporters: Importer01:27

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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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The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

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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.
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Membrane Asymmetry Regulating Transporters01:19

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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...
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Structure of Porins01:21

Structure of Porins

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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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Author Spotlight: A Bicelle Crystallization Setup for ABC Transporter Membrane Proteins to Advance Drug Development
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Structure of a dimeric full-length ABC transporter.

Sarah C Bickers1,2, Samir Benlekbir3, John L Rubinstein4,5,6

  • 1Department of Chemistry, University of Toronto, Toronto, ON, Canada.

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|November 16, 2024
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Summary
This summary is machine-generated.

Researchers reveal the structure of a yeast ABC transporter (Ycf1p) dimer, showing lipids stabilize it and affect its function. This finding offers insights into ABCC protein dimerization.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • ATP-binding cassette (ABC) proteins are crucial transporters regulated by various mechanisms.
  • Oligomerization, including dimerization, is a proposed regulatory mechanism for ABC proteins, but high-resolution structures are lacking.

Purpose of the Study:

  • To determine the high-resolution structure of the mature yeast cadmium factor 1 (Ycf1p), an ABCC subfamily member.
  • To investigate the functional implications of Ycf1p dimerization.

Main Methods:

  • X-ray crystallography to determine the structure of cleaved Ycf1p.
  • Biochemical assays to compare monomeric and dimeric Ycf1p phosphorylation and ATPase activity.

Main Results:

  • The mature Ycf1p exists as both monomers and a well-ordered dimer in solution.
  • The Ycf1p dimer exhibits reduced phosphorylation and ATPase activity compared to the monomer.
  • Lipids are present at the dimer interface, suggesting a role in stabilizing the dimer.

Conclusions:

  • This study provides the first high-resolution structure of an ABCC dimer, revealing lipid-mediated stabilization.
  • Dimerization significantly impacts Ycf1p function, specifically its regulatory phosphorylation and ATPase activity.
  • The Ycf1p dimer structure serves as a model for understanding dimerization in other ABCC proteins.