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ATP Synthase - Crossref

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Last Updated: 10 August 2022

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Structural basis of proton translocation and force generation in mitochondrial ATP synthase

ATP synthases synthase ATP by rotary catalysis, aided by the membrane's electrochemical proton gradient. By electron cryo-microscopy at near-atomic resolution, we established the structure of an intact mitochondrial ATP synthase dimer. Two aqueous channels are identified by Charges and polar residues of the a-subunit stator's polar residues, each covering one half of the membrane. The protonated glutamate meets the matrix channel and deprotonates on ring rotation.

Source link: https://doi.org/10.7554/elife.33274


Structure and function of the intermembrane space domain of mammalian F o F 1 ATP synthase

Introduction Mitochondrial F o F 1 synthase is a membrane-bound molecular machine integral to cell energy conversion and cristae architecture. Two distinct 3D structures of monomeric bovine F o F 1 ATP synthase by single particle cryo-electron microscopy differ by the presence and absence of the IMD. Comparison of both structures reveals that the IMD is a bipartite and weakly associated domain of F o F 1 ATP synthase. We compare the current structure of the mammalian IMD in the bovine F o F 1 ATP synthase monomer with structures of dimeric F o F 1 ATP synthase synthase, demonstrating that the IMD is a common yet structurally divergent feature of several mitochondrial ATP synthases.

Source link: https://doi.org/10.1101/193045


Mutational analysis of a conserved positive charge in the c -ring of E. coli ATP synthase

The electrochemical gradient of protons is turned into rotation by the membrane-embedded F o motor, which is then used to drive conformational transitions in the soluble F 1 motor that catalyzes ATP synthesis. The F o motor is mounted on a ring in E. coli with subpoena a, facilitating proton transport. Arg50 and Thr51 on the cytoplasmic side of each subunit c are involved in the proton translocation process, according to previous research, and positive charge is conserved in this region of subunit c. We produced eleven mutant mutants and assayed their in vitro ATP synthesis, H+ pumping, and passive H+ permeability activities, as well as the ability of mutants to carry out oxidative phosphorylation in vivo to determine the role of these residues and the physical characteristics of these positions.

Source link: https://doi.org/10.1101/2022.07.28.501891


Enhanced abundance and activity of the chloroplast ATP synthase in rice through the overexpression of the AtpD subunit

Chloroplast ATP synthase produces ATP with the proton motive force created by solar energy-driven thylakoid electron transport reactions. Here we investigate how rising supply of ATP synthase affects leaf photosynthesis and rice production, a variety of Oryza sativa Kitaake. When a stepwise rise in CO2 partial pressure was introduced on leaves of high irradiance, plants with elevated AtpD content had higher CO2 assimilation rates. Despite a wild type-like abundance of the Cytochrome b6f complex, measurements of assimilation revealed that plants overexpressing AtpD had a higher electron transport rate at high CO2 at high CO2, suggesting that plants overexpressing AtpD had a higher electron transfer rate at high CO2 in high CO2. Both in transgenic plants, the higher maximum carboxylation rate and lower cyclic electron flow indicate increased ATP production as compared to wild type plants. Our results reveal that the rate of electron transport at elevated CO2 and high irradiance can be modulated by ATP synthase, according to our findings.

Source link: https://doi.org/10.1093/jxb/erac320


Bacterial F-type ATP synthases follow a well-choreographed assembly pathway

Although the basic chemistry of several ATPases is established today, the precise assembly route for F 1 F O -ATP synthases is mostly unclear. We investigated the self-assembly of purified proteins in a variety of environments to investigate Acetobacterium woodii's bacterial F1 assembly. In addition, we provide a roadmap for the assembly path for the assembly of a functional F1 complex.

Source link: https://doi.org/10.21203/rs.3.rs-146068/v1


DJ-1 interacts with the ectopic ATP-synthase in endothelial cells during acute ischemia and reperfusion

Endothelial cells play a vital role in ischemia. During acute ischemia and I/R in ECs, we focused on the characterization of DJ-1's endothelial dynamics and its involvement in the control of the ectopic ATP-synthase activity. By a device that is enhanced in ischemia and I/R, we found that DJ-1 is hidden from ECs. DJ-1, a cleaved version of DJ-1, was discovered only in the mysterious genome of ischemic cells. The inhibition of DJ-1 expression stifled the ecATP-S response to ischemia by 52%, and its exogenous administration maximized the effect, along with an improved Akt phosphorylation and angiotube-formation potential at reperfusion. The ecATP-S research demonstrated a close relationship between DJ-1 and the ecATP-S. During acute ischemia and reperfusion, Altogether's report reveals that DJ-1 is actively cleared and released from ischemic ECs, and plays a vital part in the regulation of ecATP-S activity during acute ischemia and reperfusion.

Source link: https://doi.org/10.1038/s41598-022-16998-3


Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states

Using cryo-electron microscopy, a molecular model that provides a framework for analyzing the wealth of functional data obtained on the E. coli F-ATP synthase has been developed. The peripheral stalk of the complex is broken for the first time in this rotary ATPase subtype's full length, revealing the F1 attachment points and a coiled-coil that bifurcates toward the membrane with its helices splitting to embrace subunits from both directions.

Source link: https://doi.org/10.7554/elife.21598

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions