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ATP Driven Pumps I: An Overview

ATP Driven Pumps I: An Overview

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 are...

ATP Synthase: Mechanism

ATP Synthase: Mechanism

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 ATP...

ATP Synthase: Structure

ATP Synthase: Structure

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...

The ADP/ATP Carrier Protein

The ADP/ATP Carrier Protein

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...

ATP Driven Pumps II: P-type Pumps

ATP Driven Pumps II: P-type Pumps

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...

ATP Driven Pumps III: V-type Pumps

ATP Driven Pumps III: V-type Pumps

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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Related Experiment Video

Updated: Jul 30, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

The structure and interactions of Ca(2+)-ATPase

A N Martonosi¹

¹Department of Biochemistry and Molecular Biology, State University of New York, Syracuse 13210, USA.

Bioscience Reports

|October 1, 1995

Summary

Calcium (Ca2+) transport by Ca(2+)-ATPase involves dynamic interactions and structural changes. A two-channel model explains Ca2+ movement across membranes during transport.

Area of Science:

Structural biology
Biochemistry
Membrane protein function

Background:

Ca(2+)-ATPase is crucial for calcium ion transport across cellular membranes.
Understanding enzyme conformation and its effect on interactions is key to elucidating transport mechanisms.

Purpose of the Study:

To investigate Ca(2+)-ATPase interactions and conformational changes during Ca2+ transport.
To correlate structural dynamics with functional states using biophysical techniques.

Main Methods:

Electron crystallography of Ca(2+)-ATPase membrane crystals.
Fourier-transform infrared (FTIR) spectroscopy triggered by photolysis of caged Ca2+.
Analysis of enzyme-ligand interactions and secondary structure modifications.

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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

Chemical Modification of the Tryptophan Residue in a Recombinant Ca²⁺-ATPase N-domain for Studying Tryptophan-ANS FRET

Published on: October 9, 2021

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle

Purification of the Sarco-Endoplasmic Reticulum Ca²⁺-ATPase from Rabbit Muscle

Published on: March 21, 2025

Related Experiment Videos

Last Updated: Jul 30, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

Chemical Modification of the Tryptophan Residue in a Recombinant Ca²⁺-ATPase N-domain for Studying Tryptophan-ANS FRET

Published on: October 9, 2021

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle

Purification of the Sarco-Endoplasmic Reticulum Ca²⁺-ATPase from Rabbit Muscle

Published on: March 21, 2025

Main Results:

Distinct ATPase-ATPase interactions observed based on enzyme conformation, influenced by Ca2+ levels and membrane potential.
Ca2+ binding induces changes in secondary structure and carboxylate groups, confirmed by FTIR.
These changes reverse during ATP hydrolysis, indicating a low-affinity phosphorylated intermediate.

Conclusions:

A two-channel model for Ca2+ translocation is proposed, involving specific membrane-spanning helices.
The model suggests separate, interacting Ca2+ binding sites facilitating ion transport.
Dynamic structural rearrangements are integral to the Ca2+ transport cycle of Ca(2+)-ATPase.