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Related Concept Videos

ATP Synthase: Structure01:18

ATP Synthase: Structure

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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...
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ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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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...
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Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
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ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

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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...
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The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

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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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AAA+ ATPases: structural insertions under the magnifying glass.

Matthew Jessop1, Jan Felix1, Irina Gutsche1

  • 1Institut de Biologie Structurale, Univ. Grenoble Alpes, CEA, CNRS, IBS, 71 Avenue des martyrs, F-38044 Grenoble, France.

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Advances in cryo-electron microscopy (cryo-EM) reveal new AAA+ ATPase structures. This structural data challenges current classifications and deepens our understanding of their diverse cellular functions and mechanisms.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • AAA+ ATPases are crucial protein machines involved in fundamental cellular processes.
  • Recent breakthroughs in cryo-electron microscopy (cryo-EM) have significantly expanded the structural data available for AAA+ ATPases.

Purpose of the Study:

  • To analyze the impact of new cryo-EM structural data on the classification of AAA+ ATPase modules.
  • To investigate the structure-function relationships of AAA+ ATPases using integrated structural and biochemical data.
  • To explore the debate surrounding a unified molecular mechanism for AAA+ ATPase activity.

Main Methods:

  • Analysis of newly available high-resolution cryo-electron microscopy (cryo-EM) structures.
  • Integration of structural findings with existing biochemical data.
  • Comparative analysis of conserved core structures and variable insertions in AAA+ proteins.

Main Results:

  • New structural insights reveal variations in AAA+ ATPase core structures, questioning current clade classifications.
  • Combined structural and biochemical data facilitate a deeper understanding of AAA+ ATPase function.
  • Evidence is presented both supporting and refuting a single, universal mechanism for AAA+ ATPase activity.

Conclusions:

  • The influx of cryo-EM data necessitates a re-evaluation of AAA+ ATPase classification.
  • Structure-function relationships are becoming clearer, though a unifying mechanism remains debated.
  • Further research is stimulated by the complex interplay between structure, function, and mechanism in AAA+ ATPases.