Evidence map›Paper›PMID 39769317›Full record

ArticleInternational journal of molecular sciences2024

Functional Roles of the Charged Residues of the C- and M-Gates in the Yeast Mitochondrial NAD

Daniela Valeria Miniero, Ferdinando Palmieri, Virginia Quadrotta, Fabio Polticelli, Luigi Palmieri, Magnus Monné

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Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Daniela Valeria MinieroDepartment of Biosciences, Biotechnology and Environment, University of Bari Aldo Moro, Via E. Orabona 4, 70125 Bari, Italy.ORCID 0000-0002-3324-9692
Ferdinando PalmieriDepartment of Biosciences, Biotechnology and Environment, University of Bari Aldo Moro, Via E. Orabona 4, 70125 Bari, Italy.
Virginia QuadrottaDepartment of Sciences, University Roma Tre, Viale G. Marconi 446, 00146 Rome, Italy.
Fabio PolticelliDepartment of Sciences, University Roma Tre, Viale G. Marconi 446, 00146 Rome, Italy.ORCID 0000-0002-7657-2019
Luigi PalmieriDepartment of Biosciences, Biotechnology and Environment, University of Bari Aldo Moro, Via E. Orabona 4, 70125 Bari, Italy.ORCID 0000-0002-6503-2922
Magnus MonnéDepartment of Biosciences, Biotechnology and Environment, University of Bari Aldo Moro, Via E. Orabona 4, 70125 Bari, Italy.ORCID 0000-0003-2344-3878

Funding

Centre of Excellence on Comparative Genomics (CEGBA)Ministero dell'Istruzione, dell'Università e della Ricerca (MIUR), PRIN 2017 2017PAB8EMMinistero dell'Istruzione, dell'Università e della Ricerca (MIUR), PRIN 2020 2020RRJP5L
6 · The paper itself

Abstract

Mitochondrial carriers transport organic acids, amino acids, nucleotides and cofactors across the mitochondrial inner membrane. These transporters consist of a three-fold symmetric bundle of six transmembrane α-helices that encircle a pore with a central substrate binding site, whose alternating access is controlled by a cytoplasmic and a matrix gate (C- and M-gates). The C- and M-gates close by forming two different salt-bridge networks involving the conserved motifs [YF][DE]XX[KR] on the even-numbered and PX[DE]XX[KR] on the odd-numbered transmembrane α-helices, respectively. We have investigated the effects on transport of mutating the C-gate charged residues of the yeast NAD

Indexed as

NADSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsBinding SitesMitochondriaMolecular Docking SimulationMutationNADSaccharomyces cerevisiae Proteinsmembrane transportmembrane transport proteinmitochondriamitochondrial carriermitochondrial transporterNAD+ carriertransport mechanism

Identifiers

PMID39769317
PMCPMC11677788

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.