ArticleBiophysical journal2009
Asymmetric conformational flexibility in the ATP-binding cassette transporter HI1470/1.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Dielectric double shell characterization of yeast cells exposed to simulated microgravity.NPJ microgravity · 2026Article
- Global comparative structural analysis of responses to protein phosphorylation.Nature communications · 2025Article
- Identification of Novel Immunogenic Proteins of Neisseria gonorrhoeae by Phage Display.PloS one · 2016Article
- The conformational transition pathways of ATP-binding cassette transporter BtuCD revealed by targeted molecular dynamics simulation.PloS one · 2012Article
- Inter-domain communication mechanisms in an ABC importer: a molecular dynamics study of the MalFGK2E complex.PLoS computational biology · 2011Article
- Capturing Functional Motions of Membrane Channels and Transporters with Molecular Dynamics Simulation.Journal of computational and theoretical nanoscience · 2010Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Putative metal-chelate-type ABC transporter HI1470/1 is homologous with vitamin B(12) importer BtuCD but exhibits a distinct inward-facing conformation in contrast to the outward-facing conformation of BtuCD. Normal-mode analysis of HI1470/1 reveals the intrinsic asymmetric conformational flexibility in this transporter and demonstrates that the transition from the inward-facing to the outward-facing conformation is realized through the asymmetric motion of individual subunits of the transporter. This analysis suggests that the asymmetric arrangement of the BtuC dimer in the crystal structure of the BtuCD-F complex represents an intermediate state relating HI1470/1 and BtuCD. Furthermore, a twisting motion between transmembrane domains and nucleotide-binding domains encoded in the lowest-frequency normal mode of this type of importer is found to contribute to the conformational transitions during the whole cycle of substrate transportation. A more complete translocation mechanism of the BtuCD type importer is proposed.
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