Dynamics in an unusual acyl carrier protein from a ladderane lipid‐synthesizing organism

Anaerobic ammonium‐oxidizing (anammox) bacteria express a distinct acyl carrier protein implicated in the biosynthesis of the highly unusual “ladderane” lipids these organisms produce. This “anammox‐specific” ACP, or amxACP, shows several unique features such as a conserved FF motif and an unusual s...

Full description

Saved in:
Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2022-01, Vol.90 (1), p.73-82
Main Authors: Dietl, Andreas, Barends, Thomas R. M.
Format: Article
Language:English
Subjects:
ACP
Acyl carrier protein
Acyl Carrier Protein - chemistry
Acyl Carrier Protein - metabolism
Amino Acid Motifs
Ammonium
Anaerobic Ammonia Oxidation
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Biosynthesis
Conserved sequence
Crystal structure
ensemble refinement
Helices
lipid biosynthesis
Lipid Metabolism
Lipids
molecular dynamics
Molecular Dynamics Simulation
Oxidation
Planctomycetes - chemistry
Prostheses
Protein biosynthesis
protein dynamics
Protein structure
Proteins
Shielding
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Anaerobic ammonium‐oxidizing (anammox) bacteria express a distinct acyl carrier protein implicated in the biosynthesis of the highly unusual “ladderane” lipids these organisms produce. This “anammox‐specific” ACP, or amxACP, shows several unique features such as a conserved FF motif and an unusual sequence in the functionally important helix III. Investigation of the protein's structure and dynamics, both in the crystal by ensemble refinement and by MD simulations, reveals that helix III adopts a rare six‐residue‐long 310‐helical conformation that confers a large degree of conformational and positional variability on this part of the protein. This way of introducing structural flexibility by using the inherent properties of 310‐helices appears unique among ACPs. Moreover, the structure suggests a role for the FF motif in shielding the thioester linkage between the protein's prosthetic group and its acyl cargo from hydrolysis.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.26187