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

Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...

You might also read

Related Articles

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

Sort by
Same author

Targeted Protein Degradation.

JACS Au·2026
Same author

Unique Microswitches Positioned Extracellular to the Orthosteric Binding Site Initiate Activation in the β<sub>1</sub>-Adrenergic Receptor.

Journal of chemical information and modeling·2026
Same author

Decision making by modular polyketide synthases and implications for genetic engineering.

Natural product reports·2026
Same author

Docking domains from modular polyketide synthases and their use in engineering.

Nature communications·2025
Same author

Protocol for the purification, analysis, and handling of acyl carrier proteins from type I fatty acid and polyketide synthases.

STAR protocols·2025
Same author

Correction: Exploiting the inherent promiscuity of the acyl transferase of the stambomycin polyketide synthase for the mutasynthesis of analogues.

Chemical science·2025

Related Experiment Video

Updated: Jul 9, 2026

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
10:40

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

Multienzyme docking in hybrid megasynthetases.

Carsten D Richter1, Daniel Nietlispach, R William Broadhurst

  • 1Department of Biochemistry, 80 Tennis Court Road, University of Cambridge, Cambridge CB2 1GA, UK. c.d.richter.03@cantab.net

Nature Chemical Biology
|December 11, 2007
PubMed
Summary
This summary is machine-generated.

Scientists discovered a new protein interaction mechanism in bacteria. This involves a novel docking domain family (TubCdd) crucial for hybrid polyketide synthase (PKS) and nonribosomal polypeptide synthetase (NRPS) assembly lines, ensuring accurate natural product biosynthesis.

More Related Videos

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach
10:01

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach

Published on: June 23, 2026

Related Experiment Videos

Last Updated: Jul 9, 2026

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
10:40

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach
10:01

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach

Published on: June 23, 2026

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Hybrid multienzyme systems, combining polyketide synthases (PKS) and nonribosomal polypeptide synthetases (NRPS), are vital for producing valuable natural products in bacteria.
  • The assembly line process relies on precise interactions between enzyme modules, mediated by terminal docking domains for fidelity.

Purpose of the Study:

  • To identify and characterize novel docking domains involved in PKS-NRPS hybrid systems.
  • To elucidate the structural basis of protein-protein recognition in these biosynthetic assembly lines.

Main Methods:

  • Identification of a new family of N-terminal docking domains, exemplified by TubCdd from the tubulysin system.
  • Nuclear Magnetic Resonance (NMR) spectroscopy to determine the three-dimensional structure of TubCdd.
  • Analysis of protein-protein interaction interfaces and residue-specific interactions.

Main Results:

  • Discovery of TubCdd, a homodimeric N-terminal docking domain from a bacterial PKS-NRPS system.
  • NMR structure reveals a novel fold with an exposed beta-hairpin acting as the binding site for partner C-terminal docking domains.
  • Identification of charged residues on the beta-hairpin as critical determinants for interaction specificity, termed a 'docking code'.

Conclusions:

  • A new family of homodimeric N-terminal docking domains (TubCdd) has been identified, playing a key role in hybrid PKS-NRPS systems.
  • The structural and biochemical data provide insights into the molecular recognition mechanism governing the assembly of these complex biosynthetic machinery.
  • The identified 'docking code' offers potential for engineering enzyme-substrate specificity and modifying natural product biosynthesis.