Related Experiment Video
Updated: May 17, 2026

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry
Published on: May 21, 2018
Post-translational modification in the archaea: structural characterization of multi-enzyme complex lipoylation
Mareike G Posner1, Abhishek Upadhyay, Susan J Crennell
1Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK.
Archaeal lipoylation involves two proteins, LplA-N and LplA-C, which fold and interact to enable lipoic acid attachment. This study reveals their functional interdependence and substrate flexibility, crucial for understanding archaeal metabolism.
Area of Science:
- Biochemistry
- Structural Biology
- Archaea
Background:
- Lipoylation is vital for metabolism, attaching lipoic acid to enzyme complexes.
- Archaeal lipoylation differs from bacterial/eukaryotic, often involving two proteins: LplA-N and LplA-C.
- The structure and function of Thermoplasma acidophilum LplA-C in lipoylation were previously unknown.
Purpose of the Study:
- To elucidate the structure and function of the archaeal lipoylation system in Thermoplasma acidophilum.
- To determine the structural and biochemical basis of LplA-N and LplA-C interaction and their roles in lipoylation.
- To investigate the substrate specificity of the archaeal lipoylation machinery.
Main Methods:
- X-ray crystallography to determine the structures of the LplA-N-LplA-C complex and the E2lipD substrate.
- Biochemical analyses to assess protein interactions, conformational changes, and enzymatic activity.
- Comparative structural analysis of archaeal LplA with bacterial and eukaryotic homologs.
Main Results:
- LplA-C is intrinsically disordered but gains structure upon binding to LplA-N, inducing conformational changes in LplA-N.
- The LplA-N-LplA-C complex exhibits a unique adenylate-binding region and interacts with E2lipD only in the presence of substrate.
- The archaeal lipoylation system can utilize both lipoic acid and octanoic acid, highlighting functional flexibility.
Conclusions:
- LplA-N and LplA-C function interdependently, with LplA-C crucial for LplA-N activity and proper complex formation.
- The findings provide insights into the mechanism of archaeal lipoylation and its evolutionary conservation.
- This study clarifies the roles of LplA-N and LplA-C in a key metabolic pathway within archaea.
More Related Videos
05:57Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations
Published on: April 26, 2024
12:11Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
Published on: February 27, 2020
Related Concept Videos
Biosynthesis of Lipids
Formation of Lipopolysaccharides
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Lipid Catabolism
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Diversity of Archaea III