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

Transcription Elongation Factors02:35

Transcription Elongation Factors

11.9K
Transcription elongation is a dynamic process that alters depending upon the sequence heterogeneity of the DNA being transcribed. Hence, it is not surprising that the elongation complex's composition also varies along the way while transcribing a gene.
The transcription elongation is regulated via pausing of RNA polymerase on several occasions during transcription. In bacteria, these halts are necessary because the transcription of DNA into mRNA is coupled to the translation of that mRNA...
11.9K
Transcription Elongation Factors02:35

Transcription Elongation Factors

4.1K
4.1K
Mechanical Protein Functions01:58

Mechanical Protein Functions

5.2K
Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
5.2K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

15.6K
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...
15.6K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

3.2K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
3.2K
Transcriptional Regulation: Riboswitches01:23

Transcriptional Regulation: Riboswitches

248
Riboswitches are RNA elements that regulate gene expression by altering their secondary structures in response to specific effector molecules. These elements, located in the leader regions of certain mRNAs, act as transcriptional regulators by toggling between alternative conformations to control downstream gene expression. Riboswitch-mediated regulation is a precise mechanism for modulating biosynthetic pathways, as exemplified by the riboflavin biosynthesis pathway in Bacillus...
248

You might also read

Related Articles

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

Sort by
Same author

Crystal structure of a complete threonyl tRNA synthetase: toggle clamp model?

Biochemical and biophysical research communications·2025
Same author

Crystal structures of Mycobacterium tuberculosis and Mycobacterium thermoresistibile glycyl-tRNA synthetases in various liganded states.

PloS one·2025
Same author

Architecture of <i>Pseudomonas aeruginosa</i> glutamyl-tRNA synthetase defines a subfamily of dimeric class Ib aminoacyl-tRNA synthetases.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Lactate dehydrogenase is the Achilles' heel of Lyme disease bacterium <i>Borreliella burgdorferi</i>.

mBio·2025
Same author

Crystal Structure, Modeling, and Identification of Key Residues Provide Insights into the Mechanism of the Key Toxoflavin Biosynthesis Protein ToxD.

Biochemistry·2025
Same author

Lactate dehydrogenase is the Achilles' heel of Lyme disease bacterium <i>Borreliella burgdorferi</i>.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Oct 29, 2025

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
10:59

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Published on: May 13, 2019

9.9K

Structural basis of elongation factor 2 switching.

Michael K Fenwick1, Steven E Ealick1

  • 1Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, 14853, USA.

Current Research in Structural Biology
|July 8, 2021
PubMed
Summary
This summary is machine-generated.

Archaebacterial and eukaryotic elongation factor 2 (EF-2) and elongation factor G (EF-G) GTPases adopt novel compact conformations. These structures suggest a previously unknown "on" ribosome-free state for these essential protein synthesis factors.

Keywords:
Elongation factorGTPaseRibosomeSwitchTranslationTranslocaseTranslocation

More Related Videos

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs
10:37

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs

Published on: May 10, 2018

12.8K
Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
12:26

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

Published on: February 12, 2022

5.3K

Related Experiment Videos

Last Updated: Oct 29, 2025

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
10:59

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Published on: May 13, 2019

9.9K
Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs
10:37

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs

Published on: May 10, 2018

12.8K
Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
12:26

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

Published on: February 12, 2022

5.3K

Area of Science:

  • Structural Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Elongation factors EF-2 and EF-G are crucial five-domain GTPases for protein synthesis.
  • Classical GTPase activation involves GDP/GTP exchange and ordering of switch I and II segments.
  • Previous crystal structures of EF-2 and EF-G did not fully explain their activation mechanism.

Purpose of the Study:

  • To elucidate the structural basis of EF-2 activation.
  • To investigate the conformational states of Methanoperedens nitroreducens EF-2 (MnEF-2).
  • To characterize MnEF-2 in complex with GMPPCP and magnesium.

Main Methods:

  • X-ray crystallography was used to determine the structures of MnEF-2 and a mutant form (MnEF-2-H595N).
  • Structures were solved in complex with the GTP analog GMPPCP and magnesium.
  • Analysis of domain interactions and structural element ordering.

Main Results:

  • Novel compact conformations of MnEF-2 and MnEF-2-H595N were observed.
  • Domain III interacts with other domains, and the overall structure resembles the spliceosomal GTPase SNU114.
  • Switch II is highly ordered, while Switch I shows variable ordering, forming part of a cation binding site.
  • An essential histidine in Switch II is positioned in an inactive conformation.

Conclusions:

  • The determined compact conformations represent a previously unreported
  • on
  • ribosome-free state.
  • These findings challenge the classical model of GTPase activation for EF-2 and EF-G.
  • The structures provide new insights into the conformational dynamics of these essential translational GTPases.