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Related Concept Videos

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Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
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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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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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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...
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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
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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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Single Liposome Measurements for the Study of Proton-Pumping Membrane Enzymes Using Electrochemistry and Fluorescent Microscopy
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Proton-driven alternating access in a spinster lipid transporter.

Reza Dastvan1, Ali Rasouli2, Sepehr Dehghani-Ghahnaviyeh2

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Spinster (Spns) transporters move sphingosine-1-phosphate (S1P) across membranes. This study reveals how protonation drives conformational changes in bacterial Spns, uncovering mechanisms for S1P transport and potential drug targets.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Transport

Background:

  • Spinster (Spns) lipid transporters are essential for cellular sphingosine-1-phosphate (S1P) transport.
  • Spns2 is a key S1P transporter in human endothelial cells, representing a potential therapeutic target for modulating S1P signaling.

Purpose of the Study:

  • To identify novel conformational states of the bacterial Hyphomonas neptunium Spns (HnSpns) transporter.
  • To elucidate the proton- and substrate-coupled conformational dynamics of HnSpns within lipid membranes.

Main Methods:

  • Integrated approach utilizing lipid membranes to study HnSpns.
  • Analysis of conserved residues involved in protonation steps and conformational transitions.
  • Investigation of a periplasmic salt bridge's role in transporter conformation.

Main Results:

  • Identified conserved residues critical for protonation and regulation of conformational changes.
  • Demonstrated sequential protonation coordinating transitions in a ligand-dependent alternating access mechanism.
  • Revealed a periplasmic salt bridge (Asp60TM2:Arg289TM7) maintaining a closed transporter conformation.

Conclusions:

  • Proton-dependent dynamics on the periplasmic side facilitate ligand exchange.
  • Understanding HnSpns conformational dynamics provides insights into S1P transport mechanisms.
  • Conserved mechanisms highlight potential strategies for targeting Spns transporters.