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Atomic Structure

Atomic Structure

The Greek philosopher Democritus proposed that everything on Earth is made up of tiny particles called atomos, Greek for "indivisible," from which the modern term "atom" is derived. In the 19th century, John Dalton proposed the atomic theory that is still largely correct today. He put forth five postulates to explain how atoms made up the world around us. (1) All matter is composed of infinitely small particles or atoms. (2) All atoms of a given element are identical to one...

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Additional Subnuclear Structures

Additional Subnuclear Structures

The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals.
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The Nucleosome Core Particle

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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Related Experiment Video

Updated: Dec 5, 2025

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Atomic structure of human TOM core complex.

Wenhe Wang¹, Xudong Chen¹, Laixing Zhang¹

¹Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology & Frontier Research Center for Biological Structure, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, 100084 Beijing, China.

|October 21, 2020

Summary

This summary is machine-generated.

The human mitochondrial protein import gate, the translocase of the outer mitochondrial membrane (TOM) complex, has been structurally elucidated. This reveals the TOM core complex

Keywords:

Cryoelectron microscopy Structural biology

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Area of Science:

Mitochondrial biology
Protein translocation
Structural biology

Background:

The translocase of the outer mitochondrial membrane (TOM) complex facilitates the import of mitochondrial proteins.
Understanding the TOM complex structure is crucial for deciphering mitochondrial protein import pathways.

Purpose of the Study:

To determine the high-resolution structure of the dimeric human TOM core complex (TOM-CC).
To elucidate the structural basis of preprotein translocation through the TOM complex.

Main Methods:

Single-particle cryo-electron microscopy (cryo-EM) was employed.
Analysis of the dimeric human TOM-CC structure.

Main Results:

The structure reveals two Tom40 β-barrel proteins forming the channel, stabilized by Tom22 subunits and a phospholipid.
Small Tom proteins (Tom5, Tom6, Tom7) adopt specific configurations around the channel.
Distinct electrostatic features, including a negative interior and peripheral positive regions, were identified.
Evidence suggests two dimeric TOM complexes can form a parallelogram-shaped tetramer.

Conclusions:

The determined structure provides atomic-level insights into the TOM complex architecture and function.
The electrostatic surface potential offers clues to the preprotein translocation mechanism.
The potential tetrameric arrangement offers a new perspective on mitochondrial protein import and Tom subunit organization.