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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...

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 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...

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...

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...

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Related Experiment Video

Updated: Jun 13, 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

Structural divergence between the two subgroups of P5 ATPases.

Danny Mollerup Sørensen¹, Morten J Buch-Pedersen, Michael Gjedde Palmgren

¹Centre for Membrane Pumps in Cells and Disease, PUMPKIN, Danish National Research Foundation, Department of Plant Biology and Biotechnology, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark.

Biochimica Et Biophysica Acta

|April 27, 2010

Summary

P5 ATPases, crucial for eukaryotic origins, are divided into P5A and P5B subgroups. Bioinformatic analysis reveals distinct structures and potential functions, highlighting differences in membrane topology and catalytic domains.

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Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

P5 type ATPases are essential but poorly understood pumps in P-type ATPases.
Phylogenetic analysis suggests two subgroups: P5A and P5B, with distinct cellular localizations and roles.

Purpose of the Study:

To bioinformatically identify sequence differences between P5A and P5B ATPases.
To elucidate structural and functional distinctions between these two P5 ATPase subgroups.

Main Methods:

Phylogenetic analysis of P5 ATPase sequences.
Bioinformatic comparison of primary sequences, focusing on membrane topology and catalytic domains.

Main Results:

P5A and P5B ATPases exhibit unique membrane topologies compared to other P-type ATPases.
Sequence conservation suggests different substrate specificities for P5A and P5B ATPases.
Identified sequence variations in catalytic domains indicate differential kinetic properties.

Conclusions:

P5A and P5B ATPases are structurally and functionally distinct subgroups.
These differences likely contribute to their varied roles in cellular processes and disease.