Structure and dynamics of human and bacterial acyl carrier proteins and their interactions with fatty acid synthesis proteins.
Acyl Carrier Protein
/ chemistry
Amino Acid Sequence
Animals
Bacterial Proteins
/ chemistry
Escherichia coli
/ chemistry
Escherichia coli Proteins
/ chemistry
Fatty Acid Synthase, Type II
/ chemistry
Fatty Acids
/ metabolism
Humans
Molecular Docking Simulation
Protein Conformation
Protein Interaction Maps
Sequence Alignment
Streptomyces coelicolor
/ chemistry
Acyl carrier protein
Acyl carrier protein synthase
Dynamics
Type I FAS
Type II FAS
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
03 09 2019
03 09 2019
Historique:
received:
29
06
2019
accepted:
05
07
2019
pubmed:
13
7
2019
medline:
2
6
2020
entrez:
13
7
2019
Statut:
ppublish
Résumé
Acyl carrier protein (ACP) is highly conserved across taxa and plays key roles in the fatty acid synthesis system by mediating acyl group delivery and shuttling. Here, we compared the structural and dynamic features of human type Ι ACP (hACP) and Escherichia coli type II ACP (EcACP). Analysis of chemical shift perturbations upon octanoyl group attachment showed perturbations in hACP only near acyl-group attachment sites, whereas EcACP showed the perturbation at residues in the hydrophobic cavity. This difference confirmed that hACP does not sequester the acyl chain in the hydrophobic cavity, which is blocked by hydrophobic triad residues (L34, L39, and V64). Moreover, hACP showed more flexible backbone dynamics than EcACP, especially in the front of α
Identifiants
pubmed: 31296387
pii: S0006-291X(19)31354-3
doi: 10.1016/j.bbrc.2019.07.018
pii:
doi:
Substances chimiques
Acyl Carrier Protein
0
Bacterial Proteins
0
Escherichia coli Proteins
0
Fatty Acids
0
acpP protein, E coli
0
Fatty Acid Synthase, Type II
EC 6.-
Types de publication
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1183-1189Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.