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Related Concept Videos

ATP Synthase: Structure01:18

ATP Synthase: Structure

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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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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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ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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Primary Active Transport01:29

Primary Active Transport

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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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Primary Active Transport01:47

Primary Active Transport

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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 that are embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction...
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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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Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
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Crystal structure of a light-driven sodium pump.

Ivan Gushchin1, Vitaly Shevchenko2, Vitaly Polovinkin1

  • 11] Institut de Biologie Structurale, Université Grenoble Alpes, Grenoble, France. [2] Institut de Biologie Structurale, Centre National de la Recherche Scientifique, Grenoble, France. [3] Institut de Biologie Structurale, Commissariat à l'Énergie Atomique (CEA), Grenoble, France. [4] Laboratory for Advanced Studies of Membrane Proteins, Moscow Institute of Physics and Technology, Dolgoprudniy, Russia. [5] Institute of Complex Systems (ICS), ICS-6, Structural Biochemistry, Research Center Jülich, Jülich, Germany.

Nature Structural & Molecular Biology
|April 8, 2015
PubMed
Summary

Researchers elucidated the structure of Krokinobacter eikastus rhodopsin 2 (KR2), a light-driven sodium pump. Structural insights reveal its ion-translocation pathway and enable engineering for new cation pump properties.

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Area of Science:

  • Structural Biology
  • Biochemistry
  • Optogenetics

Background:

  • Microbial rhodopsins are a family of light-driven ion pumps.
  • The first light-driven sodium pumps were recently discovered within this family.
  • Understanding their structure is key to harnessing their potential.

Purpose of the Study:

  • To determine the high-resolution structures of Krokinobacter eikastus rhodopsin 2 (KR2) in different functional states.
  • To elucidate the ion-translocation pathway and key structural features of KR2.
  • To explore the potential for engineering KR2 for novel cation-pumping functions.

Main Methods:

  • X-ray crystallography was used to solve the structures of KR2.
  • High-resolution structures were obtained for the monomeric blue state and two pentameric red states.
  • Site-directed mutagenesis was employed to investigate functional changes.

Main Results:

  • The structures revealed the complete ion-translocation pathway of KR2.
  • Key structural features, including the sodium ion binding site at the oligomerization interface and a unique N-terminal helix capping the release cavity, were identified.
  • A mutation (G263F) was found to confer potassium-pumping activity to KR2.

Conclusions:

  • The determined structures provide unprecedented insight into the mechanism of light-driven sodium pumps.
  • KR2's unique structural features facilitate cation translocation and can be rationally engineered.
  • These findings are valuable for the development of optogenetic tools and novel cation transporters.