ArticleJournal of the American Chemical Society2013
The structure of the mercury transporter MerF in phospholipid bilayers: a large conformational rearrangement results from N-terminal truncation.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- A Minimal Membrane Metal Transport System: Dynamics and Energetics of mer Proteins.Journal of computational chemistry · 2020Article
- New applications of solid-state NMR in structural biology.Emerging topics in life sciences · 2018Article
- Cloning, Expression, Isotope Labeling, and Purification of Transmembrane Protein MerF from Mercury ResistantFrontiers in microbiology · 2017Article
- Dynamic Nuclear Polarization as an Enabling Technology for Solid State Nuclear Magnetic Resonance Spectroscopy.Analytical chemistry · 2016Article
- Chemical speciation of MeHgChemical science · 2015Article
- Amphipols outperform dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase.Analytical chemistry · 2015Article
- Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Membrane protein structure from rotational diffusion.Biochimica et biophysica acta · 2015Review
- Structure of the membrane protein MerF, a bacterial mercury transporter, improved by the inclusion of chemical shift anisotropy constraints.Journal of biomolecular NMR · 2014Article
- Solid-state NMR structure determination from diagonal-compensated, sparsely nonuniform-sampled 4D proton-proton restraints.Journal of the American Chemical Society · 2014Article
- NMR structures of membrane proteins in phospholipid bilayers.Quarterly reviews of biophysics · 2014Review
- Mechanism of dilute-spin-exchange in solid-state NMR.The Journal of chemical physics · 2014Article
- Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.Journal of biomolecular NMR · 2014Article
- Sampling scheme and compressed sensing applied to solid-state NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013Article
- Structure determination of membrane proteins in their native phospholipid bilayer environment by rotationally aligned solid-state NMR spectroscopy.Accounts of chemical research · 2013Article
- The development of solid-state NMR of membrane proteins.Biomedical spectroscopy and imagingArticle
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Authors and funding
5 authors.
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Abstract
The three-dimensional structure of the 81-residue mercury transporter MerF determined in liquid crystalline phospholipid bilayers under physiological conditions by Rotationally Aligned (RA) solid-state NMR has two long helices, which extend well beyond the bilayer, with a well-defined interhelical loop. Truncation of the N-terminal 12 residues, which are mobile and unstructured when the protein is solubilized in micelles, results in a large structural rearrangement of the protein in bilayers. In the full-length protein, the N-terminal helix is aligned nearly parallel to the membrane normal and forms an extension of the first transmembrane helix. By contrast, this helix adopts a perpendicular orientation in the truncated protein. The close spatial proximity of the two Cys-containing metal binding sites in the three-dimensional structure of full-length MerF provides insights into possible transport mechanisms. These results demonstrate that major changes in protein structure can result from differences in amino acid sequence (e.g., full-length vs truncated proteins) as well as the use of a non-native membrane mimetic environment (e.g., micelles) vs liquid crystalline phospholipid bilayers. They provide further evidence of the importance of studying unmodified membrane proteins in near-native bilayer environments in order to obtain accurate structures that can be related to their functions.
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