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A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

DOI

  • Mathias Weber, Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität, Tyskland
  • Lydia Tome, Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität, Tyskland
  • Daniel Otzen
  • Dirk Schneider, Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität, Tyskland
When localized adjacent to a Pro-kink, Thr and Ser residues can form hydrogen bonds between their polar hydroxyl group and a backbone carbonyl oxygen and thereby modulate the actual bending angle of a distorted transmembrane α-helix. We have used the homo-dimeric transmembrane cytochrome b(559)' to analyze the potential role of a highly conserved Ser residue for assembly and stabilization of transmembrane proteins. Mutation of the conserved Ser residue to Ala resulted in altered heme binding properties and in increased stability of the holo-protein, most likely by tolerating subtle structural rearrangements upon heme binding. The results suggest a crucial impact of an intrahelical Ser hydrogen bond in defining the structure of a Pro-kinked transmembrane helix dimer.
OriginalsprogEngelsk
TidsskriftBBA General Subjects
Vol/bind1818
Nummer9
Sider (fra-til)2103-7
Antal sider5
ISSN0304-4165
DOI
StatusUdgivet - 2012

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