Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
Protein Families02:47

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key locations, protein...
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Non-canonical subunit functions in multiprotein complexes: insights from the Mediator complex.

Biochemical Society transactions·2026
Same author

Sec Signal Peptide Doubles Up as a Leader Sequence in Bufferin Biosynthesis.

ACS chemical biology·2026
Same author

CrpH of <i>Bordetella pertussis</i>, a prototypic PepSY_TM protein supporting heme-copper oxidoreductase function.

Frontiers in microbiology·2026
Same author

Bacteria gain a firm hold in the airways.

Science (New York, N.Y.)·2026
Same author

Structural basis of human Mediator recruitment by the phosphorylated transcription factor Elk-1.

Nature communications·2025
Same author

A new biofunctionalized and micropatterned PDMS is able to promote stretching induced human myotube maturation.

Lab on a chip·2025

Related Experiment Video

Updated: Jun 22, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

First structural insights into the TpsB/Omp85 superfamily.

Françoise Jacob-Dubuisson1, Vincent Villeret, Bernard Clantin

  • 1INSERM U629, Institut Pasteur de Lille, 1 rue Calmette, F-59019 Lille cedex, France. francoise.jacob@ibl.fr

Biological Chemistry
|June 30, 2009
PubMed
Summary

Proteins like FhaC transport molecules across bacterial outer membranes and have similar roles in eukaryotic organelles. Understanding FhaC

More Related Videos

From Constructs to Crystals &#8211; Towards Structure Determination of &#946;-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

F&#246;rster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features
07:09

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

Published on: March 16, 2022

Related Experiment Videos

Last Updated: Jun 22, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

From Constructs to Crystals &#8211; Towards Structure Determination of &#946;-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

F&#246;rster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features
07:09

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

Published on: March 16, 2022

Area of Science:

  • Microbiology and Structural Biology
  • Cell Biology

Background:

  • Proteins of the TpsB/Omp85 superfamily are crucial for protein transport and assembly in the outer membranes of Gram-negative bacteria.
  • Eukaryotic homologs of these proteins perform analogous functions in chloroplasts and mitochondria.

Purpose of the Study:

  • To elucidate the mechanism of action of TpsB transporters.
  • To understand the structural basis of protein transport across outer membranes.

Main Methods:

  • X-ray crystallography of the FhaC transporter.

Main Results:

  • The X-ray structure of FhaC, a representative TpsB transporter, was determined.
  • FhaC possesses conserved structural features including POTRA domains, a transmembrane beta barrel, and a functional loop.

Conclusions:

  • The structure of FhaC provides a foundation for understanding the broader TpsB/Omp85 superfamily.
  • Conserved structural elements are key to the function of these essential transport proteins.