How metal cofactors drive dimer-dodecamer transition of the M42 aminopeptidase TmPep1050 of
Amino Acid Sequence
Aminopeptidases
/ chemistry
Bacterial Proteins
/ chemistry
Biocatalysis
Catalytic Domain
Cobalt
/ metabolism
Coenzymes
/ metabolism
Conserved Sequence
Enzyme Stability
Ions
Models, Molecular
Protein Multimerization
Protein Structure, Secondary
Temperature
Thermotoga maritima
/ enzymology
M42 aminopeptidase
aminopeptidase
bacteria
metalloprotease
oligomerization
oligomerization shift
protein assembly
protein complex
protein folding
protein stability
protein structure
thermophile
thermostability
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
22 11 2019
22 11 2019
Historique:
received:
09
05
2019
revised:
24
09
2019
pubmed:
16
10
2019
medline:
11
6
2020
entrez:
16
10
2019
Statut:
ppublish
Résumé
The M42 aminopeptidases are dinuclear aminopeptidases displaying a peculiar tetrahedron-shaped structure with 12 subunits. Their quaternary structure results from the self-assembly of six dimers controlled by their divalent metal ion cofactors. The oligomeric-state transition remains debated despite the structural characterization of several archaeal M42 aminopeptidases. The main bottleneck is the lack of dimer structures, hindering the understanding of structural changes occurring during the oligomerization process. We present the first dimer structure of an M42 aminopeptidase, TmPep1050 of
Identifiants
pubmed: 31611236
pii: S0021-9258(20)30355-0
doi: 10.1074/jbc.RA119.009281
pmc: PMC6879339
doi:
Substances chimiques
Bacterial Proteins
0
Coenzymes
0
Ions
0
Cobalt
3G0H8C9362
Aminopeptidases
EC 3.4.11.-
Banques de données
PDB
['6NW5', '4P6Y', '5NE6', '1YLO', '5NE7', '5NE8']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
17777-17789Informations de copyright
© 2019 Dutoit et al.
Déclaration de conflit d'intérêts
The authors declare that they have no conflicts of interest with the contents of this article.
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