Probing the Transmembrane Structure and Topology of Microsomal Cytochrome-P450 by Solid-State NMR on Temperature-Resistant Bicelles
Identifieur interne : 000462 ( Main/Merge ); précédent : 000461; suivant : 000463Probing the Transmembrane Structure and Topology of Microsomal Cytochrome-P450 by Solid-State NMR on Temperature-Resistant Bicelles
Auteurs : Kazutoshi Yamamoto ; Melissa Gildenberg [États-Unis] ; Shivani Ahuja [États-Unis] ; Sang-Choul Im [États-Unis] ; Paige Pearcy [États-Unis] ; Lucy Waskell [États-Unis] ; Ayyalusamy Ramamoorthy [États-Unis]Source :
- Scientific Reports [ 2045-2322 ] ; 2013.
Abstract
Though the importance of high-resolution structure and dynamics of membrane proteins has been well recognized, optimizing sample conditions to retain the native-like folding and function of membrane proteins for Nuclear Magnetic Resonance (NMR) or X-ray measurements has been a major challenge. While bicelles have been shown to stabilize the function of membrane proteins and are increasingly utilized as model membranes, the loss of their magnetic-alignment at low temperatures makes them unsuitable to study heat-sensitive membrane proteins like cytochrome-P450 and protein-protein complexes. In this study, we report temperature resistant bicelles that can magnetically-align for a broad range of temperatures and demonstrate their advantages in the structural studies of full-length microsomal cytochrome-P450 and cytochrome-b5 by solid-state NMR spectroscopy. Our results reveal that the N-terminal region of rabbit cytochromeP4502B4, that is usually cleaved off to obtain crystal structures, is helical and has a transmembrane orientation with ~17° tilt from the lipid bilayer normal.
Url:
DOI: 10.1038/srep02556
PubMed: 23989972
PubMed Central: 3757361
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Transmembrane Structure and Topology of Microsomal Cytochrome-P450 by Solid-State NMR on Temperature-Resistant Bicelles</title><author><name sortKey="Yamamoto, Kazutoshi" sort="Yamamoto, Kazutoshi" uniqKey="Yamamoto K" first="Kazutoshi" last="Yamamoto">Kazutoshi Yamamoto</name><affiliation><nlm:aff id="a1"><institution>Biophysics and Department of Chemistry, University of Michigan</institution>, Ann Arbor, MI 48109-1055</nlm:aff><wicri:noCountry code="subfield">MI 48109-1055</wicri:noCountry></affiliation></author><author><name sortKey="Gildenberg, Melissa" sort="Gildenberg, Melissa" uniqKey="Gildenberg M" first="Melissa" last="Gildenberg">Melissa Gildenberg</name><affiliation wicri:level="2"><nlm:aff id="a1"><institution>Biophysics and Department of Chemistry, University of Michigan</institution>, Ann Arbor, MI 48109-1055</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Michigan</region></placeName><wicri:cityArea>, Ann Arbor</wicri:cityArea></affiliation></author><author><name sortKey="Ahuja, Shivani" sort="Ahuja, Shivani" uniqKey="Ahuja S" first="Shivani" last="Ahuja">Shivani Ahuja</name><affiliation wicri:level="2"><nlm:aff id="a1"><institution>Biophysics and Department of Chemistry, University of Michigan</institution>, Ann Arbor, MI 48109-1055</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Michigan</region></placeName><wicri:cityArea>, Ann Arbor</wicri:cityArea></affiliation></author><author><name sortKey="Im, Sang Choul" sort="Im, Sang Choul" uniqKey="Im S" first="Sang-Choul" last="Im">Sang-Choul Im</name><affiliation wicri:level="2"><nlm:aff id="a1"><institution>Biophysics and Department of Chemistry, University of Michigan</institution>, Ann Arbor, MI 48109-1055</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Michigan</region></placeName><wicri:cityArea>, Ann Arbor</wicri:cityArea></affiliation><affiliation 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Anesthesiology, University of Michigan, and VA Medical Center</institution>, Ann Arbor, MI</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Michigan</region></placeName><wicri:cityArea>, Ann Arbor</wicri:cityArea></affiliation></author><author><name sortKey="Ramamoorthy, Ayyalusamy" sort="Ramamoorthy, Ayyalusamy" uniqKey="Ramamoorthy A" first="Ayyalusamy" last="Ramamoorthy">Ayyalusamy Ramamoorthy</name><affiliation wicri:level="2"><nlm:aff id="a1"><institution>Biophysics and Department of Chemistry, University of Michigan</institution>, Ann Arbor, MI 48109-1055</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Michigan</region></placeName><wicri:cityArea>, Ann Arbor</wicri:cityArea></affiliation></author></analytic><series><title level="j">Scientific Reports</title><idno type="eISSN">2045-2322</idno><imprint><date 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While bicelles have been shown to stabilize the function of membrane proteins and are increasingly utilized as model membranes, the loss of their magnetic-alignment at low temperatures makes them unsuitable to study heat-sensitive membrane proteins like cytochrome-P450 and protein-protein complexes. In this study, we report temperature resistant bicelles that can magnetically-align for a broad range of temperatures and demonstrate their advantages in the structural studies of full-length microsomal cytochrome-P450 and cytochrome-b5 by solid-state NMR spectroscopy. Our results reveal that the N-terminal region of rabbit cytochromeP4502B4, that is usually cleaved off to obtain crystal structures, is helical and has a transmembrane orientation with ~17° tilt from the lipid bilayer normal.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Rasmussen, S G" uniqKey="Rasmussen S">S. G. 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Philpot</name></author><author><name sortKey="Coon, M J" uniqKey="Coon M">M. J. Coon</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Zhang, Y" uniqKey="Zhang Y">Y. Zhang</name></author><author><name sortKey="Kucukural, A" uniqKey="Kucukural A">A. Kucukural</name></author><author><name sortKey="Zhang, Y" uniqKey="Zhang Y">Y. Zhang</name></author></analytic></biblStruct></listBibl></div1></back></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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