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Related Concept Videos

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...
The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate filaments...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Energy to Drive Translocation01:37

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.

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Related Experiment Video

Updated: Jul 11, 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

Three-dimensional structure of the Tn5 synaptic complex transposition intermediate.

D R Davies1, I Y Goryshin, W S Reznikoff

  • 1Department of Biochemistry, University of Wisconsin, Madison, WI 53706, USA.

Science (New York, N.Y.)
|July 7, 2000
PubMed
Summary

DNA transposition, a key driver of genomic evolution, is facilitated by transposases. This study reveals the 3D structure of Tn5 transposase bound to DNA, offering insights into transposition mechanisms.

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Area of Science:

  • Molecular Biology
  • Genomics
  • Structural Biology

Background:

  • DNA transposition is a fundamental biological process influencing genome evolution.
  • Transposases and retroviral integrases, like HIV-1 integrase, catalyze transposition and integration events.
  • Understanding the DNA-protein interactions is crucial for elucidating transposition mechanisms.

Discussion:

  • The study presents the 3D structure of prokaryotic Tn5 transposase complexed with Tn5 transposon end DNA at 2.3 angstrom resolution.
  • The dimeric molecular assembly shows each DNA molecule bound by both protein subunits, positioning transposon ends within active sites.
  • This structure elucidates DNA binding, cleavage, hairpin intermediate formation, and strand transfer during transposition.

Key Insights:

  • The structure reveals how Tn5 transposase binds and cleaves DNA, involving distinct subunits for binding and catalysis.
  • It demonstrates the formation of a hairpin intermediate during DNA cleavage by a single active site.
  • The findings provide a molecular basis for understanding the strand transfer step into target DNA.

Outlook:

  • This structural information can guide the development of novel gene-editing tools and therapeutic strategies targeting transposition.
  • Further research can explore the dynamics of the transposase-DNA complex and its interactions with target DNA.
  • Comparative structural studies can illuminate the evolution and diversity of transposition mechanisms across different organisms.