Question

pls explain ATP synthase'functions and its structure??

Answer 1

HI mate GM here is your answer...,

ATP synthase is an enzyme that directly generates adenosine triphosphate (ATP) during the process of cellular respiration. The function of ATP synthase is to produce ATP. ATP is necessary to power all cellular processes, so it is constantly being used by cells and constantly needs to be produced. Each ATP synthase can produce about 100 molecules of ATP every second. Eukaryotes, such as plants, animals, and fungi, have organelles called mitochondria that mainly function as ATP producers. Plants also have chloroplasts that contain ATP synthase and can produce ATP from sunlight and carbon dioxide. Bacteria and archaea, which make up the prokaryotes, do not have mitochondria but produce ATP through similar cellular respiration processes in their plasma membrane. Across all forms of life, ATP synthase has basically the same structure and function. Therefore, it is thought to have evolved early on in the evolution of life, and would have been found in the last common ancestor of all life on Earth.

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Answer 2

structure of ATp synthase:The F1-ATPase from Trypanosoma brucei. The α-,  β-, γ-, δ-, ε-, and p18 subunits are red, yellow, blue, green, magenta and cyan respectively. (A and B) Cartoon representations of the side and top views; (C-E) surface representations of (C), the bovine F1-ATPase, (D), the T. brucei enzyme in grey with p18 removed and the coloured sections showing the amino acids additional to the bovine enzyme, and (E), the T. brucei enzyme with p18 present. 

The structures and functions of the components of ATP synthases, especially those subunits involved directly in the catalytic formation of ATP, are widely conserved in metazoans, fungi, eubacteria and plant chloroplasts. On the basis of a map at 32.5 Å resolution determined in situ in the mitochondria of the euglenozoan parasite, Trypanosoma brucei, by electron cryo-tomography, it has been proposed that the ATP synthase in this species has a non-canonical structure with different catalytic sites, where the catalytically essential arginine-finger is provided, not by the α-subunit adjacent to the catalytic nucleotide binding site, as in all species investigated to date, but by a protein called p18 found only in the euglenozoa [34]. In a collaboration with Drs Alena Zíková and Ondřej Gahura from the Institute of Parasitology at České Budějovice in the Czech Republic, we have characterized the F1-ATPase from T. brucei [35] and determined a crystal structure of the enzyme at 3.2 Å resolution [36]. This structure shows that the proposal that the catalytic domain of this ATP synthase has a non-canonical structure and different catalytic sites is incorrect. In many respects, the structure of the T. brucei F1-ATPase is closely similar to those of F1-ATPases determined previously. The α3β3-spherical portion of the catalytic domain, where the three catalytic sites are found, plus the central stalk, are highly conserved, and the arginine finger is provided conventionally by the α-subunits adjacent to each of the three catalytic sites found in the β-subunits. Thus, the enzyme has a conventional catalytic mechanism. The structure differs from earlier ones by having a p18-subunit, identified only in the euglenozoa, associated with the external surface of each of the three α-subunits, thereby elaborating the F1-domain. Subunit p18 is a pentatricopeptide repeat (PPR) protein [37] with three PPRs and appears to have no function in the catalytic mechanism of the enzyme. T. brucei is the causative agent of sleeping sickness in humans and related diseases in domestic animals living in Sub-Saharan Africa, and the structure of its F1-ATPases provides a target for development
function of ATP synthase :
function of ATP synthase is to produce ATP. ATP is necessary to power all cellular processes, so it is constantly being used by cells and constantly needs to be produced. Each ATP synthase can produce about 100 molecules of ATP every second. Eukaryotes, such as plants, animals, and fungi, have organelles called mitochondria that mainly function as ATP producers. Plants also have chloroplasts that contain ATP synthase and can produce ATP from sunlight and carbon dioxide. Bacteria and archaea, which make up the prokaryotes, do not have mitochondria but produce ATP through similar cellular respiration processes in their plasma membrane. Across all forms of life, ATP synthase has basically the same structure and function. Therefore, it is thought to have evolved early on in the evolution of life, and would have been found in the last common ancestor of all life on Earth.