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Related Concept Videos

Secondary Active Transport01:32

Secondary Active Transport

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One example of how cells use the energy contained in electrochemical gradients is demonstrated by glucose transport into cells. The ion vital to this process is sodium (Na+), which is typically present in higher concentrations extracellularly than in the cytosol. Such a concentration difference is due, in part, to the action of an enzyme "pump" embedded in the cellular membrane that actively expels Na+ from a cell. Importantly, as this pump contributes to the high concentration of...
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Secondary Active Transport01:55

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One example of how cells use the energy contained in electrochemical gradients is demonstrated by glucose transport into cells. The ion vital to this process is sodium (Na+), which is typically present in higher concentrations extracellularly than in the cytosol. Such a concentration difference is due, in part, to the action of an enzyme “pump” embedded in the cellular membrane that actively expels Na+ from a cell. Importantly, as this pump contributes to the high concentration of...
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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.
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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

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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Drug Absorption Mechanism: Carrier-Mediated Membrane Transport01:19

Drug Absorption Mechanism: Carrier-Mediated Membrane Transport

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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.
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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

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Structural and Energetic Analysis of the CmABCB1 Substrate Transport.

Kei Moritsugu1,2, Ryuji Ishida2, Takumi Someya2

  • 1Graduate School of Science, Osaka Metropolitan University, 1-2 Gakuen-cho, Naka-ku, Sakai, Osaka 599-8570, Japan.

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|October 4, 2025
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This study reveals how P-glycoprotein (P-gp) transports molecules using free energy landscapes. ATP binding drives conformational changes, facilitating substrate release and cellular efflux.

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Author Spotlight: A Bicelle Crystallization Setup for ABC Transporter Membrane Proteins to Advance Drug Development
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • P-glycoprotein (P-gp), an ABCB1 transporter, effluxes hydrophobic compounds via conformational changes.
  • Crystal structures of its homologue (CmABCB1) suggest transport involves transmembrane helix (TMH) and nucleotide-binding domain (NBD) movements.

Purpose of the Study:

  • To compute the minimum free energy path (MFEP) for the P-gp inward-facing (IF) to outward-facing (OF) transition.
  • To elucidate the structural and energetic basis of rhodamine 6G (R6G) transport using crystallographic data.

Main Methods:

  • Employed the string method to calculate the MFEP of the IF-to-OF conformational transition.
  • Analyzed the role of ATP binding, NBD dimerization, and substrate interactions.

Main Results:

  • ATP binding and NBD dimerization overcome energy barriers, disrupting the aromatic hydrophobic network (AHN).
  • This facilitates substrate binding and leads to an intermediate substrate-occluded (Occ) state.
  • Substrate interactions destabilize the Occ state, promoting transition to the OF conformation via TMH motions.

Conclusions:

  • MFEP-based free energy landscapes effectively reveal membrane transporter molecular mechanisms.
  • The study details the step-by-step process of P-gp mediated substrate transport.