A New Mechanism for High-Affinity Uptake of C4-Dicarboxylates in Bacteria Revealed by the Structure of Rhodopseudomonas palustris MatC (RPA3494), a Periplasmic Binding Protein of the Tripartite Tricarboxylate Transporter (TTT) Family.


Journal

Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R

Informations de publication

Date de publication:
18 01 2019
Historique:
received: 24 09 2018
revised: 14 11 2018
accepted: 14 11 2018
pubmed: 25 11 2018
medline: 3 3 2020
entrez: 25 11 2018
Statut: ppublish

Résumé

C4-dicarboxylates play a central role in cellular physiology as key metabolic intermediates. Under aerobic conditions, they participate in the citric acid cycle, while in anaerobic bacteria, they are important in energy-conserving fermentation and respiration processes. Ten different families of secondary transporters have been described to participate in C4-dicarboxylate movement across biological membranes, but only one of these utilizes an extracytoplasmic solute binding protein to achieve high-affinity uptake. Here, we identify the MatBAC system from the photosynthetic bacterium Rhodopseudomonas palustris as the first member of the tripartite tricarboxylate transport family to be involved in C4-dicarboxylate transport. Tryptophan fluorescence spectroscopy showed that MatC, the periplasmic binding protein from this system, binds to l- and d-malate with K

Identifiants

pubmed: 30471256
pii: S0022-2836(18)30977-X
doi: 10.1016/j.jmb.2018.11.016
pii:
doi:

Substances chimiques

Bacterial Proteins 0
Carrier Proteins 0
Fumarates 0
Malates 0
Membrane Transport Proteins 0
Periplasmic Binding Proteins 0
citrate-binding transport protein 0
malic acid 817L1N4CKP
Succinic Acid AB6MNQ6J6L

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

351-367

Informations de copyright

Copyright © 2018 The Authors. Published by Elsevier Ltd.. All rights reserved.

Auteurs

Leonardo T Rosa (LT)

Department of Molecular Biology and Biotechnology, The University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.

Samuel R Dix (SR)

Department of Molecular Biology and Biotechnology, The University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.

John B Rafferty (JB)

Department of Molecular Biology and Biotechnology, The University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.

David J Kelly (DJ)

Department of Molecular Biology and Biotechnology, The University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK. Electronic address: d.kelly@sheffield.ac.uk.

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Classifications MeSH