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 Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.8K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.8K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.1K
2.1K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.4K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.4K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.4K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.4K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

1.9K
1.9K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.5K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.5K

You might also read

Related Articles

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

Sort by
Same author

Biochemical characterization and structural insights of trehalose-6-phosphate phosphatases from Stenotrophomonas maltophilia and Xanthomonas axonopodis.

Biochemical and biophysical research communications·2026
Same author

Safety and Feasibility of Pulsed Field Ablation With a Pentaspline Catheter in Patients With Extravascular ICD.

Pacing and clinical electrophysiology : PACE·2026
Same author

Manipulation of nonclassical ubiquitin signaling by pathogenic bacteria.

Current opinion in microbiology·2026
Same author

Genetic and epigenetic mechanisms underlying male reproductive thermotolerance.

Current opinion in plant biology·2026
Same author

Phenotypic characterization of signature-tagged mutants identifies physiological determinants of <i>Vibrio vulnificus</i> fitness.

Applied and environmental microbiology·2026
Same author

Novel bisphosphonate derivative partially attenuates iron-associated oxidative stress in doxorubicin-induced testicular injury.

Reproductive toxicology (Elmsford, N.Y.)·2026

Related Experiment Video

Updated: Dec 20, 2025

Applying Live Cell Imaging and Cryo-Electron Tomography to Resolve Spatiotemporal Features of the Legionella pneumophila Dot/Icm Secretion System
09:12

Applying Live Cell Imaging and Cryo-Electron Tomography to Resolve Spatiotemporal Features of the Legionella pneumophila Dot/Icm Secretion System

Published on: March 10, 2020

7.5K

Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex.

Hyunmin Kim1, Tomoko Kubori2, Kohei Yamazaki2,3

  • 1Department of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea.

Nature Communications
|May 28, 2020
PubMed
Summary

The Dot/Icm type IVB coupling protein (T4CP) complex in Legionella pneumophila selectively exports effector proteins. Structural analysis reveals how LvgA within T4CP recognizes diverse effector binding motifs, clarifying substrate specificity.

More Related Videos

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.8K
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.6K

Related Experiment Videos

Last Updated: Dec 20, 2025

Applying Live Cell Imaging and Cryo-Electron Tomography to Resolve Spatiotemporal Features of the Legionella pneumophila Dot/Icm Secretion System
09:12

Applying Live Cell Imaging and Cryo-Electron Tomography to Resolve Spatiotemporal Features of the Legionella pneumophila Dot/Icm Secretion System

Published on: March 10, 2020

7.5K
Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.8K
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.6K

Area of Science:

  • Microbiology
  • Structural Biology
  • Molecular Biology

Background:

  • Legionella pneumophila utilizes the Dot/Icm type IVB secretion system (T4BSS) to translocate approximately 300 effector proteins into host cells.
  • The Dot/Icm type IVB coupling protein (T4CP) complex, comprising IcmS, IcmW, and LvgA, is crucial for the selective export of specific effector subclasses.

Purpose of the Study:

  • To elucidate the structural basis of effector recognition by the Dot/Icm T4CP complex.
  • To investigate the substrate-binding specificities of the LvgA subunit within the T4CP complex.

Main Methods:

  • X-ray crystallography was employed to determine the structure of a T4CP subcomplex bound to the effector protein VpdB.
  • Mutational analyses were performed to identify and characterize effector binding motifs recognized by LvgA.

Main Results:

  • The crystal structure revealed a direct interaction between LvgA and a C-terminal linear motif of the effector VpdB.
  • LvgA's binding interface was found to interact with the C-terminal regions of three additional effectors: SidH, SetA, and PieA.
  • Mutational studies identified a shared FxxxLxxxK binding motif in VpdB and SidH, indicating LvgA recognizes multiple distinct binding motifs.

Conclusions:

  • This study provides a structural foundation for understanding how the Dot/Icm T4CP complex recognizes and binds to its diverse effector substrates.
  • The findings highlight the adaptable substrate-binding capabilities of the LvgA adaptor subunit, essential for the T4BSS's functional versatility.