Isolated Heme A Synthase from Aquifex aeolicus Is a Trimer.
Aquifex aeolicus
cofactor biosynthesis
heme A synthase
hyperthermophilic bacterium
metalloproteins
protein oligomerization
respiratory chain
structural biology
Journal
mBio
ISSN: 2150-7511
Titre abrégé: mBio
Pays: United States
ID NLM: 101519231
Informations de publication
Date de publication:
30 06 2020
30 06 2020
Historique:
entrez:
2
7
2020
pubmed:
2
7
2020
medline:
10
4
2021
Statut:
epublish
Résumé
The integral membrane protein heme A synthase (HAS) catalyzes the biosynthesis of heme A, which is a prerequisite for cellular respiration in a wide range of aerobic organisms. Previous studies have revealed that HAS can form homo-oligomeric complexes, and this oligomerization appears to be evolutionarily conserved among prokaryotes and eukaryotes and is shown to be essential for the biological function of eukaryotic HAS. Despite its importance, little is known about the detailed structural properties of HAS oligomers. Here, we aimed to address this critical issue by analyzing the oligomeric state of HAS from
Identifiants
pubmed: 32605991
pii: mBio.02615-19
doi: 10.1128/mBio.02615-19
pmc: PMC7327177
pii:
doi:
Substances chimiques
Bacterial Proteins
0
CtaA protein, bacteria
0
Cytochrome b Group
0
Membrane Proteins
0
heme a
18535-39-2
Heme
42VZT0U6YR
Oxygen
S88TT14065
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2020 Zeng et al.
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