ArticleProceedings of the National Academy of Sciences of the United States of America2013
A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 33 citations in OpenAlex.
- When less is more: Counterintuitive stoichiometries and cellular abundances are essential for ABC transporters' function.Science advances · 2025Article
- Review
- Substrate recognition and ATPase activity of theThe Journal of biological chemistry · 2020Article
- Indole Reverses Intrinsic Antibiotic Resistance by Activating a Novel Dual-Function Importer.mBio · 2019Article
- The Different Effects of Substrates and Nucleotides on the Complex Formation of ABC Transporters.Structure (London, England : 1993) · 2019Article
- Single-molecule probing of the conformational homogeneity of the ABC transporter BtuCD.Nature chemical biology · 2018Article
- ATP binding and hydrolysis disrupt the high-affinity interaction between the heme ABC transporter HmuUV and its cognate substrate-binding protein.The Journal of biological chemistry · 2017Article
- Rad50 ATPase activity is regulated by DNA ends and requires coordination of both active sites.Nucleic acids research · 2017Article
- L-glutamine Induces Expression of Listeria monocytogenes Virulence Genes.PLoS pathogens · 2017Article
- Article
- The Klebsiella pneumoniae O12 ATP-binding Cassette (ABC) Transporter Recognizes the Terminal Residue of Its O-antigen Polysaccharide Substrate.The Journal of biological chemistry · 2016Article
- The uncoupled ATPase activity of the ABC transporter BtuC2D2 leads to a hysteretic conformational change, conformational memory, and improved activity.Scientific reports · 2016Article
- ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations.PloS one · 2016Article
- Toward Determining ATPase Mechanism in ABC Transporters: Development of the Reaction Path-Force Matching QM/MM Method.Methods in enzymology · 2016Article
- Conformational Motions and Functionally Key Residues for Vitamin B12 Transporter BtuCD-BtuF Revealed by Elastic Network Model with a Function-Related Internal Coordinate.International journal of molecular sciences · 2015Article
- The allosteric regulatory mechanism of the Escherichia coli MetNI methionine ATP binding cassette (ABC) transporter.The Journal of biological chemistry · 2015Article
- Identification of functionally important conserved trans-membrane residues of bacterial PIB -type ATPases.Molecular microbiology · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In all kingdoms of life, ATP binding cassette (ABC) transporters are essential to many cellular functions. In this large superfamily of proteins, two catalytic sites hydrolyze ATP to power uphill substrate translocation. A central question in the field concerns the relationship between the two ATPase catalytic sites: Are the sites independent of one another? Are both needed for function? Do they function cooperatively? These issues have been resolved for type I ABC transporters but never for a type II ABC transporter. The many mechanistic differences between type I and type II ABC transporters raise the question whether in respect to ATP hydrolysis the two subtypes are similar or different. We have addressed this question by studying the Escherichia coli vitamin B12 type II ABC transporter BtuCD. We have constructed and purified a series of BtuCD variants where both, one, or none of the ATPase sites were rendered inactive by mutation. We find that, in a membrane environment, the ATPase sites of BtuCD are highly cooperative with a Hill coefficient of 2. We also find that, when one of the ATPase sites is inactive, ATP hydrolysis and vitamin B12 transport by BtuCD is reduced by 95%. These exact features are also shared by the archetypical type I maltose ABC transporter. Remarkably, mutants that have lost 95% of their ATPase and transport capabilities still retain the ability to fully use vitamin B12 in vivo. The results demonstrate that, despite the many differences between type I and type II ABC transporters, the fundamental mechanism of ATP hydrolysis remains conserved.
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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.