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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

7.4K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.4K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

16.0K
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...
16.0K
ATP Synthase: Structure01:18

ATP Synthase: Structure

16.3K
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...
16.3K
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

5.2K
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...
5.2K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

4.9K
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...
4.9K
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

6.8K
During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
6.8K

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関連する実験動画

Updated: May 5, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
10:39

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

33.9K

ホモメール環のATPアゼにおけるインターサブユニット調整.

Jeffrey R Moffitt1, Yann R Chemla, K Aathavan

  • 1Department of Physics and Jason L. Choy Laboratory of Single Molecule Biophysics, University of California, Berkeley, California 94720, USA.

Nature
|January 9, 2009
PubMed
まとめ

研究者は,バクテリオファージ phi29のDNAパッケージングモーター,リングATPaaseを直接観察しました. 彼らはDNAを2.5塩基対のステップで包装し,サイクルごとに10塩基対を合計し,新しい調整メカニズムを明らかにすることを発見しました.

さらに関連する動画

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
12:07

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

Published on: October 9, 2021

2.6K

関連する実験動画

Last Updated: May 5, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
10:39

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

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Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
12:07

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

Published on: October 9, 2021

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科学分野:

  • バイオケミストリー バイオケミストリー
  • 分子生物学は分子生物学である.
  • 構造生物学 構造生物学とは

背景:

  • ホモメール環のATPアゼは,多様な細胞プロセスに関与する重要な分子モーターである.
  • それらのメカニズム,特にサブユニット間の調整とステップサイズを理解することは,それらの機能を明らかにする鍵です.

研究 の 目的:

  • バクテリオファージ phi29 DNA パッケージングモーターのインターサブユニット調整とステップサイズを直接観察し,定量化します.
  • 単一分子レベルでDNA転位のメカニズムを調査する.

主な方法:

  • 高解像度の光学ピンチを使って,力を加え,phi29モーターの正確な動きを測定しました.
  • 停留時間の統計分析を行い,個々のステップを解決するために高い力を適用しました.

主要な成果:

  • 10塩基対 (bp) の離散的なインクリメントで観察されたDNAパッケージング.
  • それぞれの10bpのインクリメントは,4つの調整された2.5-bpのステップで構成されていることが明らかになりました.
  • 複数のATP分子が結合し,それぞれの包装中に水解することを示した.

結論:

  • phi29モーターは,そのサブユニット間で高度に調整された水解サイクルを示しており,これはリングATPアゼのための新しいメカニズムです.
  • 非整数のステップサイズは,モーター-DNA相互作用のための新しいモデルの開発を必要とします.