Related Experiment Video
Updated: Nov 6, 2025
10:21
Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
24.5K
Structural insight into Pichia pastoris fatty acid synthase
Joseph S Snowden1, Jehad Alzahrani1, Lee Sherry1
1Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Scientific Reports
|May 8, 2021
Summary
Researchers determined the structure of yeast fatty acid synthase (FAS), a key enzyme for biofuel production. This structural insight aids in engineering FAS for novel product synthesis.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Type I fatty acid synthases (FASs) are crucial metabolic enzymes.
- FASs are targets for bioengineering in biofuel and chemical production.
- Pichia pastoris is a widely used system for protein expression.
Purpose of the Study:
- To determine the structure of P. pastoris FAS.
- To identify structural and enzymatic differences compared to S. cerevisiae FAS.
- To provide a resource for engineering yeast FAS.
Main Methods:
- Cryo-electron microscopy (cryo-EM) was used to obtain the dataset.
- Focused classification was employed to resolve mobile domains.
- The structure of P. pastoris FAS was determined to 3.1 Å resolution.
Main Results:
- The overall organization of P. pastoris FAS is typical of type I FASs.
- Several differences were identified in structural and enzymatic domains compared to S. cerevisiae FAS.
- The mobile acyl-carrier protein (ACP) domain was resolved and modeled.
Conclusions:
- The determined structure of P. pastoris FAS provides valuable insights.
- This structure will facilitate future bioengineering efforts for P. pastoris FAS.
- The findings contribute to the understanding of FAS enzymes and their engineering potential.
Related Concept Videos
01:28Overview of Fatty Acid Metabolism
32.9K
Lipids also are sources of energy that power cellular processes. Like carbohydrates, lipids are composed of carbon, hydrogen, and oxygen, but these atoms are arranged differently. Most lipids are nonpolar and hydrophobic. Major types include fats and oils, waxes, phospholipids, and steroids.
Fatty acids are catabolized in a process called beta-oxidation, which takes place in the matrix of the mitochondria and converts their fatty acid chains into two-carbon units of acetyl groups. The acetyl...
Fatty acids are catabolized in a process called beta-oxidation, which takes place in the matrix of the mitochondria and converts their fatty acid chains into two-carbon units of acetyl groups. The acetyl...
32.9K
01:29Biosynthesis of Lipids
241
Microbial membranes exhibit remarkable diversity in lipid composition, reflecting evolutionary adaptations to various environmental conditions. The three domains of life—Bacteria, Archaea, and Eukarya—synthesize membrane lipids through distinct biosynthetic pathways, leading to fundamental structural differences that impact membrane stability, function, and adaptability.Fatty Acid-Based Lipids in Bacteria and EukaryaBacteria and eukaryotes share a common fatty acid biosynthesis...
241
01:18ATP Synthase: Structure
13.9K
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...
13.9K
01:19Formation of Lipopolysaccharides
207
Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin,...
207
01:48ATP Synthase: Mechanism
15.7K
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...
15.7K
01:57Protein Complexes with Interchangeable Parts
2.7K
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...
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...
2.7K