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Related Concept Videos

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 Driven Pumps I: An Overview01:27

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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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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

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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 III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

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V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
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Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
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Copper-transporting P-type ATPases use a unique ion-release pathway.

Magnus Andersson1, Daniel Mattle2, Oleg Sitsel3

  • 11] Department of Physiology and Biophysics, University of California at Irvine, Irvine, California, USA. [2] [3].

Nature Structural & Molecular Biology
|December 10, 2013
PubMed
Summary

Heavy metal transport in cells involves PIB-type ATPases. New research reveals a copper ion (Cu(+)) release pathway in Legionella pneumophila Cu(+)-ATPase (LpCopA), explaining disease mutations and suggesting new therapeutic targets.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • PIB-type ATPases are crucial for regulating heavy metals within cells.
  • The copper-transporting ATPase from Legionella pneumophila (LpCopA) was previously characterized, with its transport pathway inferred to be occluded.

Purpose of the Study:

  • To investigate the mechanism of copper ion (Cu(+)) transport and release in LpCopA.
  • To elucidate the structural basis for Cu(+)-ATPase function and its relation to human diseases and pathogen inhibition.

Main Methods:

  • Molecular dynamics simulations to model ion solvation and pathway accessibility.
  • X-ray crystallography to determine the structure of LpCopA in the E2P state.
  • Site-directed mutagenesis and activity assays to validate the functional role of the identified pathway.

Main Results:

  • Molecular dynamics simulations indicated extracellular water solvating the transmembrane domain, suggesting a Cu(+)-release pathway.
  • A new crystal structure of LpCopA in the E2P state revealed the same ion passage.
  • Mutagenesis data supported the functional significance of this conduit for ion transport.

Conclusions:

  • The identified ion pathway provides a mechanism for Cu(+) extrusion across the membrane.
  • Structural insights explain mutations associated with Menkes' and Wilson's diseases.
  • The pathway represents a potential target for developing inhibitors against pathogenic bacteria.