Formate-nitrite transporters carrying nonprotonatable amide amino acids instead of a central histidine maintain pH-dependent transport.
Bacillus thuringiensis
/ chemistry
Bacterial Proteins
/ chemistry
Biological Transport
Entamoeba histolytica
/ chemistry
Entamoebiasis
/ parasitology
Formates
/ metabolism
Histidine
/ chemistry
Humans
Hydrogen-Ion Concentration
Models, Molecular
Nitrites
/ metabolism
Protozoan Proteins
/ chemistry
Substrate Specificity
Bacillus
Entamoeba histolytica
acetate
electron microscopy (EM)
formate
lactic acid
liposome
malaria
membrane biophysics
membrane transport
proton motive force
proton transfer
protozoan
transporter
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:
11 01 2019
11 01 2019
Historique:
received:
18
10
2018
revised:
09
11
2018
pubmed:
21
11
2018
medline:
6
5
2019
entrez:
21
11
2018
Statut:
ppublish
Résumé
Microbial formate-nitrite transporter-type proteins (FNT) exhibit dual transport functionality. At neutral pH, electrogenic anion currents are detectable, whereas upon acidification transport of the neutral, protonated monoacid predominates. Physiologically, FNT-mediated proton co-transport is vital when monocarboxylic acid products of the energy metabolism, such as l-lactate, are released from the cell. Accordingly,
Identifiants
pubmed: 30455351
pii: S0021-9258(20)40376-X
doi: 10.1074/jbc.RA118.006340
pmc: PMC6333897
doi:
Substances chimiques
Bacterial Proteins
0
Formates
0
Nitrites
0
Protozoan Proteins
0
Histidine
4QD397987E
Banques de données
PDB
['3q7k']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
623-631Informations de copyright
© 2019 Helmstetter et al.
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