ArticleThe Journal of biological chemistry2013
ATP alone triggers the outward facing conformation of the maltose ATP-binding cassette transporter.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- DeFrND: detergent-free reconstitution into native nanodiscs with designer membrane scaffold peptides.Nature communications · 2025Article
- Circularized fluorescent nanodiscs for probing protein-lipid interactions.Communications biology · 2022Article
- One-step construction of circularized nanodiscs using SpyCatcher-SpyTag.Nature communications · 2021Article
- ATP hydrolysis and nucleotide exit enhance maltose translocation in the MalFGKScientific reports · 2021Article
- Developing Nanodisc-ID for label-free characterizations of membrane proteins.Communications biology · 2021Article
- Negative Stain Single-particle EM of the Maltose Transporter in Nanodiscs Reveals Asymmetric Closure of MalKThe Journal of biological chemistry · 2017Article
- Crystal structure of bacterial haem importer complex in the inward-facing conformation.Nature communications · 2016Article
- Formation of a Chloride-conducting State in the Maltose ATP-binding Cassette (ABC) Transporter.The Journal of biological chemistry · 2016Article
- Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter.Molecular microbiology · 2015Article
- Sequential Action of MalE and Maltose Allows Coupling ATP Hydrolysis to Translocation in the MalFGK2 Transporter.The Journal of biological chemistry · 2015Article
- Conformational dynamics in substrate-binding domains influences transport in the ABC importer GlnPQ.Nature structural & molecular biology · 2015Article
- Nucleotide-free MalK drives the transition of the maltose transporter to the inward-facing conformation.The Journal of biological chemistry · 2014Article
- Structural diversity of ABC transporters.The Journal of general physiology · 2014Review
- Phosphatidylglycerol directs binding and inhibitory action of EIIAGlc protein on the maltose transporter.The Journal of biological chemistry · 2013Article
- An integrated transport mechanism of the maltose ABC importer.Research in microbiologyReview
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The maltose transporter MalFGK(2) is a study prototype for ABC importers. During catalysis, the MalFG membrane domain alternates between inward and outward facing conformations when the MalK dimer closes and hydrolyzes ATP. Because a rapid ATP hydrolysis depends on MalE and maltose, it has been proposed that closed liganded MalE facilitates the transition to the outward facing conformation. Here we find that, in contrast to the expected, ATP is sufficient for the closure of MalK and for the conversion of MalFG to the outward facing state. The outward facing transporter binds MalE with nanomolar affinity, yet neither MalE nor maltose is necessary or facilitates the transition. Thus, the rapid hydrolysis of ATP observed in the presence of MalE and maltose is not because closed liganded MalE accelerates the formation of the outward facing conformation. These findings have fundamental implications for the description of the transport reaction.
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