Mutational widening of constrictions in a formate-nitrite/H


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:
01 2022
Historique:
received: 04 10 2021
revised: 14 12 2021
accepted: 16 12 2021
pubmed: 21 12 2021
medline: 29 4 2022
entrez: 20 12 2021
Statut: ppublish

Résumé

The unrelated protein families of the microbial formate-nitrite transporters (FNTs) and aquaporins (AQP) likely adapted the same protein fold through convergent evolution. FNTs facilitate weak acid anion/H

Identifiants

pubmed: 34929166
pii: S0021-9258(21)01323-5
doi: 10.1016/j.jbc.2021.101513
pmc: PMC8749060
pii:
doi:

Substances chimiques

Anions 0
Aquaporins 0
Formates 0
Membrane Transport Proteins 0
Nitrites 0
Proton-Coupled Folate Transporter 0
Water 059QF0KO0R
formic acid 0YIW783RG1
Histidine 4QD397987E

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

101513

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.

Auteurs

Jana D R Schmidt (JDR)

Department of Pharmaceutical and Medicinal Chemistry, Christian-Albrechts-University of Kiel, Kiel, Germany.

Eric Beitz (E)

Department of Pharmaceutical and Medicinal Chemistry, Christian-Albrechts-University of Kiel, Kiel, Germany. Electronic address: ebeitz@pharmazie.uni-kiel.de.

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Classifications MeSH