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

Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Determination of Crystal Structures01:29

Determination of Crystal Structures

In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...
X-ray Crystallography02:18

X-ray Crystallography

The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
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...

You might also read

Related Articles

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

Sort by
Same author

Evolution of N-terminal mechanical lability as a determinant for Type III secretion.

Protein science : a publication of the Protein Society·2026
Same author

A Type III secretion system effector evolved to be mechanically labile and initiate unfolding from the N-terminus.

bioRxiv : the preprint server for biology·2026
Same author

A fluorescent reporter and single-turnover kinetics reveal new insight into BAM complex function.

bioRxiv : the preprint server for biology·2025
Same author

Synthesis of Nucleotide Diphosphate Uronic Acids via the Coupling of Activated Nucleotides with Uronic Acid-1-phosphates.

The Journal of organic chemistry·2025
Same author

Structure and Function of ArnD. A Deformylase Essential for Lipid A Modification with 4-Amino-4-deoxy-l-arabinose and Polymyxin Resistance.

Biochemistry·2023
Same author

Targeting the Conformational Change in ArnA Dehydrogenase for Selective Inhibition of Polymyxin Resistance.

Biochemistry·2023

Related Experiment Video

Updated: Jun 27, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
09:15

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Crystal structure of YaeT: conformational flexibility and substrate recognition.

Petia Z Gatzeva-Topalova1, Troy A Walton, Marcelo C Sousa

  • 1Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO 80309, USA.

Structure (London, England : 1993)
|December 17, 2008
PubMed
Summary

Researchers determined the crystal structure of a key bacterial outer membrane protein fragment, YaeT (E. coli Omp85). This structure reveals flexibility important for inserting other proteins into the outer membrane.

More Related Videos

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

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
10:45

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip

Published on: March 20, 2021

Related Experiment Videos

Last Updated: Jun 27, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
09:15

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

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

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
10:45

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip

Published on: March 20, 2021

Area of Science:

  • Structural biology
  • Microbiology
  • Biochemistry

Background:

  • Gram-negative bacteria possess a complex envelope with inner and outer membranes.
  • The outer membrane (OM) utilizes integral membrane proteins (OMPs) with beta-barrel domains.
  • Omp85 proteins are essential for OMP biogenesis in the OM.

Purpose of the Study:

  • To elucidate the structural basis of Omp85 function.
  • To investigate the mechanism of OMP folding and insertion into the bacterial outer membrane.

Main Methods:

  • X-ray crystallography was used to determine the structure of a periplasmic fragment of YaeT (E. coli Omp85).
  • The fragment contained the first four polypeptide transport-associated (POTRA) domains.
  • Solution X-ray scattering data was used for comparison.

Main Results:

  • The crystal structure revealed a periplasmic fragment of YaeT in an extended conformation.
  • Conformational flexibility was identified at a hinge region between POTRA2 and POTRA3 domains.
  • The structure provides insights into potential substrate binding and protein folding mechanisms.

Conclusions:

  • The determined structure of the YaeT periplasmic fragment offers a mechanistic view of OMP insertion.
  • Understanding Omp85 structure and flexibility is crucial for deciphering outer membrane protein biogenesis.