Comparative biochemical and structural analysis of the flavin-binding dodecins from
Bacterial Proteins
/ chemistry
Binding Sites
Crystallography, X-Ray
Flavin Mononucleotide
/ metabolism
Flavin-Adenine Dinucleotide
/ metabolism
Hydrogen-Ion Concentration
Membrane Transport Proteins
/ chemistry
Models, Molecular
Mutagenesis, Site-Directed
Protein Multimerization
Protein Stability
Riboflavin
/ analogs & derivatives
Species Specificity
Streptomyces
/ chemistry
Streptomyces coelicolor
/ chemistry
Temperature
Streptomyces davaonensis
dodecin
riboflavin
roseoflavin
Journal
Microbiology (Reading, England)
ISSN: 1465-2080
Titre abrégé: Microbiology (Reading)
Pays: England
ID NLM: 9430468
Informations de publication
Date de publication:
10 2019
10 2019
Historique:
pubmed:
25
7
2019
medline:
11
2
2020
entrez:
25
7
2019
Statut:
ppublish
Résumé
Dodecins are small flavin-binding proteins that are widespread amongst haloarchaeal and bacterial species. Haloarchaeal dodecins predominantly bind riboflavin, while bacterial dodecins have been reported to bind riboflavin-5'-phosphate, also called flavin mononucleotide (FMN), and the FMN derivative, flavin adenine dinucleotide (FAD). Dodecins form dodecameric complexes and represent buffer systems for cytoplasmic flavins. In this study, dodecins of the bacteria
Identifiants
pubmed: 31339487
doi: 10.1099/mic.0.000835
doi:
Substances chimiques
Bacterial Proteins
0
Membrane Transport Proteins
0
riboflavin-binding protein
0
Flavin-Adenine Dinucleotide
146-14-5
roseoflavin
51093-55-1
Flavin Mononucleotide
7N464URE7E
Riboflavin
TLM2976OFR
Types de publication
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM