ArticleBiophysical journal2008
The conformational coupling and translocation mechanism of vitamin B12 ATP-binding cassette transporter BtuCD.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025Review
- The uncoupled ATPase activity of the ABC transporter BtuC2D2 leads to a hysteretic conformational change, conformational memory, and improved activity.Scientific reports · 2016Article
- Evaluation of a Novel Tc-99m Labelled Vitamin B12 Derivative for Targeting Escherichia coli and Staphylococcus aureus In Vitro and in an Experimental Foreign-Body Infection Model.Molecular imaging and biology · 2015Article
- 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
- Identification of motions in membrane proteins by elastic network models and their experimental validation.Methods in molecular biology (Clifton, N.J.) · 2012Article
- The conformational transition pathways of ATP-binding cassette transporter BtuCD revealed by targeted molecular dynamics simulation.PloS one · 2012Article
- Capturing Functional Motions of Membrane Channels and Transporters with Molecular Dynamics Simulation.Journal of computational and theoretical nanoscience · 2010Article
- Mechanism of cohesin loading onto chromosomes: a conformational dynamics study.Biophysical journal · 2010Article
- Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins.Chemical reviews · 2010Review
- Asymmetric conformational flexibility in the ATP-binding cassette transporter HI1470/1.Biophysical journal · 2009Article
- Structural insights into ABC transporter mechanism.Current opinion in structural biology · 2008Review
- Structure, function, and evolution of bacterial ATP-binding cassette systems.Microbiology and molecular biology reviews : MMBR · 2008Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ATP-binding cassette transporter BtuCD mediating vitamin B(12) uptake in Escherichia coli couples the energy of ATP hydrolysis to the translocation of vitamin B(12) across the membrane into the cell. Elastic normal mode analysis of BtuCD demonstrates that the simultaneous substrate trapping at periplasmic cavity and ATP binding at the ATP-binding cassette (BtuD) dimer proceeds readily along the lowest energy pathway. The transport power stroke is attributed to ATP-hydrolysis-induced opening of the nucleotide-binding domain dimer, which is coupled to conformational rearrangement of transmembrane domain (BtuC) helices leading to the closing at the periplasmic side and opening at the cytoplasmic gate. Simultaneous hydrolysis of two ATP is supported by the fact that antisymmetric movement of BtuD dimer implying alternating hydrolysis cannot induce effective conformational change of the translocation pathway. A plausible mechanism of translocation cycle is proposed in which the possible effect of the association of periplasmic binding protein BtuF to the transporter is also considered.
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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.