ArticleThe EMBO journal2005
H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB.
Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers.
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154 citing papers in PubMed, 323 citations in OpenAlex.
- RecBCD Prevents Bacterial Autoimmunity by Clearing Self-DNA Ends Produced During Replication Termination.bioRxiv : the preprint server for biology · 2026Article
- Bidirectional communication between nucleotide and substrate binding sites in a type IV multidrug ABC transporter.Nature communications · 2025Article
- Structure guided functional analysis of the S. cerevisiae Mre11 complex.Nature communications · 2025Article
- The Evolution of ABC Importers.Journal of molecular biology · 2025Review
- Mapping the Role of P-gp in Multidrug Resistance: Insights from Recent Structural Studies.International journal of molecular sciences · 2025Review
- Cryo-EM analyses unveil details of mechanism and targocil-II mediated inhibition of S. aureus WTA transporter TarGH.Nature communications · 2025Article
- Magnesium enhances aurintricarboxylic acid's inhibitory action on the plasma membrane CaScientific reports · 2024Article
- Ivacaftor-Mediated Potentiation of ABCB4 Missense Mutations Affecting Critical Motifs of the NBDs: Repositioning Perspectives for Hepatobiliary Diseases.International journal of molecular sciences · 2023Article
- Evolutionary origin and sequence signatures of the heterodimeric ABCG5/ABCG8 transporter.Protein science : a publication of the Protein Society · 2022Article
- Extended-ensemble docking to probe dynamic variation of ligand binding sites during large-scale structural changes of proteins.Chemical science · 2022Article
- New insights into the resistance mechanism for the BceAB-type transporter SaNsrFP.Scientific reports · 2022Article
- Investigations on the substrate binding sites of hemolysin B, an ABC transporter, of a type 1 secretion system.Frontiers in microbiology · 2022Article
- The ABCT31 Transporter Regulates the Export System of Phenylacetic Acid as a Side-Chain Precursor of Penicillin G inFrontiers in microbiology · 2022Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- The crystal structure of the CmABCB1 G132V mutant, which favors the outward-facing state, reveals the mechanism of the pivotal joint between TM1 and TM3.Protein science : a publication of the Protein Society · 2021Article
- Quantitative real-time analysis of the efflux by the MacAB-TolC tripartite efflux pump clarifies the role of ATP hydrolysis within mechanotransmission mechanism.Communications biology · 2021Article
- Active participation of membrane lipids in inhibition of multidrug transporter P-glycoprotein.Chemical science · 2021Article
- Conformational changes in the nucleotide-binding domains of P-glycoprotein induced by ATP hydrolysis.FEBS letters · 2021Article
- Cryo-EM structure of the full-length WzmWzt ABC transporter required for lipid-linked O antigen transport.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Structure and Mechanism of Drug Transporters.Methods in molecular biology (Clifton, N.J.) · 2021Article
94 more citing papers are in PubMed but not listed here.
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5 authors at 2 institutions in 2 countries.
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Abstract
The ABC transporter HlyB is a central element of the HlyA secretion machinery, a paradigm of Type I secretion. Here, we describe the crystal structure of the HlyB-NBD (nucleotide-binding domain) with H662 replaced by Ala in complex with ATP/Mg2+. The dimer shows a composite architecture, in which two intact ATP molecules are bound at the interface of the Walker A motif and the C-loop, provided by the two monomers. ATPase measurements confirm that H662 is essential for activity. Based on these data, we propose a model in which E631 and H662, highly conserved among ABC transporters, form a catalytic dyad. Here, H662 acts as a 'linchpin', holding together all required parts of a complicated network of interactions between ATP, water molecules, Mg2+, and amino acids both in cis and trans, necessary for intermonomer communication. Based on biochemical experiments, we discuss the hypothesis that substrate-assisted catalysis, rather than general base catalysis might operate in ABC-ATPases.
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