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

ATP Synthase: Structure01:18

ATP Synthase: Structure

15.8K
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...
15.8K
Internal Loadings in Structural Members: Problem Solving01:28

Internal Loadings in Structural Members: Problem Solving

1.7K
When designing or analyzing a structural member, it is important to consider the internal loadings developed within the member. These internal loadings include normal force, shear force, and bending moment. Engineers can ensure that the structural member can support the applied external forces by calculating these internal loadings.
To illustrate this, let's consider a beam OC of 5 kN, inclined at an angle of 53.13° with the horizontal and supported at both ends. Determine the internal...
1.7K
Structure and Organization of Smooth Muscles01:13

Structure and Organization of Smooth Muscles

8.9K
Smooth muscle tissue is a type of muscle tissue that can be found lining various vital organs in the human body, including the lungs, blood vessels, digestive tract, and respiratory tract. This type of tissue is responsible for regulating the movements of these organs, playing crucial roles in the functioning of various systems, including the vascular, digestive, respiratory, and urinary systems.
Structure of smooth muscle cell
Smooth muscle cells are spindle-shaped with tapering ends and a...
8.9K
Prokaryotic Gene Structure and Organization01:28

Prokaryotic Gene Structure and Organization

2.3K
Prokaryotic genomes exhibit a streamlined organization of coding and non-coding regions essential for gene expression and protein synthesis. While coding regions contain the genetic instructions for proteins or functional RNAs, non-coding regions regulate the precise transcription and translation of these genes.Coding Regions: Proteins and RNAsThe primary coding regions, known as structural genes, include sequences transcribed into messenger RNA (mRNA) and ultimately translated into...
2.3K
Structural Organization of the Human Body: An Overview01:18

Structural Organization of the Human Body: An Overview

30.0K
It is convenient to consider the body's structures in terms of fundamental levels of organization that increase in complexity: subatomic particles, atoms, molecules, organelles, cells, tissues, organs, organ systems, and organisms.
To study the chemical level of organization, scientists consider the simplest building blocks of matter: subatomic particles, atoms, and molecules. All matter in the universe is composed of one or more unique pure substances called elements, familiar examples of...
30.0K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

17.3K
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...
17.3K

You might also read

Related Articles

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

Sort by
Same author

Acid Versus Amide-Facts and Fallacies: A Case Study in Glycomimetic Ligand Design.

Molecules (Basel, Switzerland)·2025
Same author

Structural Basis for 3-Amino-3-carboxypropyl Transfer in Nocardicin Biosynthesis.

Journal of the American Chemical Society·2025
Same author

A multichaperone condensate enhances protein folding in the endoplasmic reticulum.

Nature cell biology·2025
Same author

l-2,3-Diaminopropionate Binding Mode of the SulM Adenylation Domain Limits Engineering Monobactam Analogue Biosynthesis with Larger Substrates.

JACS Au·2025
Same author

Architecture and conformational dynamics of the BAM-SurA holo insertase complex.

Science advances·2025
Same author

Phi-Value and NMR Structural Analysis of a Coupled Native-State Prolyl Isomerization and Conformational Protein Folding Process.

Biomolecules·2025

Related Experiment Video

Updated: Feb 12, 2026

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
12:38

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction

Published on: August 9, 2011

17.9K

The structural organization of substrate loading in iterative polyketide synthases.

Dominik A Herbst1, Callie R Huitt-Roehl2, Roman P Jakob1

  • 1Department of Biozentrum, University of Basel, Basel, Switzerland.

Nature Chemical Biology
|April 4, 2018
PubMed
Summary
This summary is machine-generated.

This study reveals how starter unit acyltransferases (SAT) integrate into polyketide synthases (PKS). Structural and cryo-EM data show asymmetric conformations critical for polyketide biosynthesis, aiding enzyme engineering.

More Related Videos

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

31.6K
DNA Origami-Mediated Substrate Nanopatterning of Inorganic Structures for Sensing Applications
08:59

DNA Origami-Mediated Substrate Nanopatterning of Inorganic Structures for Sensing Applications

Published on: September 27, 2019

12.1K

Related Experiment Videos

Last Updated: Feb 12, 2026

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
12:38

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction

Published on: August 9, 2011

17.9K
Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

31.6K
DNA Origami-Mediated Substrate Nanopatterning of Inorganic Structures for Sensing Applications
08:59

DNA Origami-Mediated Substrate Nanopatterning of Inorganic Structures for Sensing Applications

Published on: September 27, 2019

12.1K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbial Metabolism

Background:

  • Polyketide synthases (PKS) are crucial microbial enzymes for producing complex secondary metabolites.
  • The initial substrate loading step in PKS is complex and involves loading modules or domains like starter unit acyltransferases (SAT).
  • The structural integration of SAT into PKS remains poorly understood.

Purpose of the Study:

  • To elucidate the structural mechanism of starter unit acyltransferase (SAT) integration into polyketide synthases (PKS).
  • To understand the structural basis of the initial substrate loading step in nonreducing PKS.

Main Methods:

  • X-ray crystallography was used to determine the structure of the loading/condensing region of the PKS CTB1.
  • Cryo-electron microscopy (cryo-EM) was employed to visualize the post-loading state of the PKS complex.
  • Mechanism-based crosslinking was utilized to trap specific enzyme conformations.

Main Results:

  • A crystal structure revealed the ordered insertion of a pseudodimeric SAT into the condensing region of PKS CTB1, facilitated by a linker.
  • Cryo-EM data showed asymmetric conformations in the CTB1 loading/condensing region, indicating preferential 1:2 binding stoichiometry.
  • These findings provide insights into the structural dynamics of the PKS loading step.

Conclusions:

  • The study clarifies the structural integration of SATs into PKS, a key step in polyketide biosynthesis.
  • Asymmetric conformations of PKS are functionally relevant and crucial for optimizing the loading process.
  • These findings are vital for re-engineering PKS for novel polyketide production.