Related Experiment Video

Updated: Jun 27, 2025

Small-Scale Plasma Membrane Preparation for the Analysis of Candida albicans Cdr1-mGFPHis
09:44

Small-Scale Plasma Membrane Preparation for the Analysis of Candida albicans Cdr1-mGFPHis

Published on: June 13, 2021

2.7K

Fungal Plasma Membrane H+-ATPase: Structure, Mechanism, and Drug Discovery

Chao-Ran Zhao1,2, Zi-Long You3, Lin Bai3

  • 1Department of Otolaryngology Head and Neck Surgery, Beijing Tongren Hospital, Capital Medical University, Beijing 100730, China.

Journal of Fungi (Basel, Switzerland)
|April 26, 2024
PubMed

Insights

The fungal plasma membrane H+-ATPase (Pma1) is a key antifungal target. Recent Cryo-EM studies reveal Pma1

Area of Science:

  • Biochemistry
  • Structural Biology
  • Mycology

Background:

  • The fungal plasma membrane H+-ATPase (Pma1) is crucial for maintaining cellular electrochemical gradients.
  • Pma1, an essential P-type ATPase in fungi, represents a promising target for antifungal drug development.
  • Understanding Pma1's structure and function is vital for combating fungal infections.

Purpose of the Study:

  • To review the historical determination of Pma1 structures.
  • To present the latest structural insights into Pma1's architecture and mechanisms.
  • To discuss current drug discovery efforts targeting Pma1.

Main Methods:

  • Review of existing literature on Pma1 structure determination.
  • Analysis of recent Cryo-Electron Microscopy (Cryo-EM) studies on Pma1.
  • Summary of antifungal drug discovery strategies targeting Pma1.

Main Results:

  • Recent Cryo-EM studies have elucidated the hexameric structure of Pma1.
  • These studies revealed Pma1's autoinhibitory and activation mechanisms.
  • Insights into the proton transport mechanism of Pma1 were provided.

Conclusions:

  • The latest structural data on Pma1 offers novel perspectives for antifungal drug design.
  • Targeting Pma1 presents a viable strategy for developing new antifungal therapies.
  • Further research into Pma1 structure-activity relationships can accelerate drug discovery.
Keywords:
drug targetfungiplasma membrane H+-ATPasestructure

More Related Videos

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle08:37

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

Published on: March 21, 2025

220
Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei08:44

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei

Published on: January 22, 2019

7.3K

Related Concept Videos

ATP Driven Pumps I: An Overview01:27

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...
8.1K
ATP Synthase: Mechanism01:48

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...
14.5K
ATP Synthase: Structure01:18

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...
12.3K
ATP Driven Pumps III: V-type Pumps01:30

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...
3.7K
Facilitated Diffusion01:16

Facilitated Diffusion

The plasma membrane, a critical structure in cellular biology, houses an array of transporters, or carrier proteins, interspersed within its lipid bilayer. These proteins play a crucial role in solute transport through facilitated diffusion, a form of passive diffusion that uses transporters to move the molecules across the membrane.
In this process, substrates such as organic compounds and ions interact with a transporter on one side, triggering conformational changes in proteins that enable...
450
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
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...
4.5K