ArticleThe Journal of biological chemistry2017
ATP binding and hydrolysis disrupt the high-affinity interaction between the heme ABC transporter HmuUV and its cognate substrate-binding protein.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Real-Time Binding Kinetics of Membrane Protein-Protein Interactions in a Membraneless Setting.Analytical chemistry · 2025Article
- The Evolution of ABC Importers.Journal of molecular biology · 2025Review
- When less is more: Counterintuitive stoichiometries and cellular abundances are essential for ABC transporters' function.Science advances · 2025Article
- Study in the iron uptake mechanism of Pasteurella multocida.Veterinary research · 2025Review
- Computational and experimental mapping of the allosteric network of two manganese ABC transporters.Protein science : a publication of the Protein Society · 2025Article
- Mechanistic insights of ABC importer HutCD involved in heme internalization by Vibrio cholerae.Scientific reports · 2022Article
- Manganese Stress Adaptation Mechanisms ofFrontiers in microbiology · 2021Article
- The Pneumococcal Iron Uptake Protein A (PiuA) Specifically Recognizes Tetradentate FeJournal of molecular biology · 2020Article
- The Different Effects of Substrates and Nucleotides on the Complex Formation of ABC Transporters.Structure (London, England : 1993) · 2019Article
- Evidence from Mutational Analysis for a Single Transmembrane Substrate Binding Site in the Histidine ATP-Binding Cassette Transporter of Salmonella enterica Serovar Typhimurium.Journal of bacteriology · 2019Article
- Heme Uptake and Utilization by Gram-Negative Bacterial Pathogens.Frontiers in cellular and infection microbiology · 2019Review
- Single-molecule probing of the conformational homogeneity of the ABC transporter BtuCD.Nature chemical biology · 2018Article
- One Intact Transmembrane Substrate Binding Site Is Sufficient for the Function of the Homodimeric Type I ATP-Binding Cassette Importer for Positively Charged Amino Acids Art(MP)Journal of bacteriology · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using the energy of ATP hydrolysis, ABC transporters catalyze the trans-membrane transport of molecules. In bacteria, these transporters partner with a high-affinity substrate-binding protein (SBP) to import essential micronutrients. ATP binding by Type I ABC transporters (importers of amino acids, sugars, peptides, and small ions) stabilizes the interaction between the transporter and the SBP, thus allowing transfer of the substrate from the latter to the former. In Type II ABC transporters (importers of trace elements,
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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.