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

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A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer. / Weber, Mathias; Tome, Lydia; Otzen, Daniel; Schneider, Dirk.

I: BBA General Subjects, Bind 1818, Nr. 9, 2012, s. 2103-7.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

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Weber, Mathias ; Tome, Lydia ; Otzen, Daniel ; Schneider, Dirk. / A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer. I: BBA General Subjects. 2012 ; Bind 1818, Nr. 9. s. 2103-7.

Bibtex

@article{56669ea08b5b4d2c9ff169fbd0d1ac65,
title = "A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer",
abstract = "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.",
author = "Mathias Weber and Lydia Tome and Daniel Otzen and Dirk Schneider",
note = "Copyright {\circledC} 2012 Elsevier B.V. All rights reserved.",
year = "2012",
doi = "10.1016/j.bbamem.2012.04.003",
language = "English",
volume = "1818",
pages = "2103--7",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier BV",
number = "9",

}

RIS

TY - JOUR

T1 - A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer

AU - Weber, Mathias

AU - Tome, Lydia

AU - Otzen, Daniel

AU - Schneider, Dirk

N1 - Copyright © 2012 Elsevier B.V. All rights reserved.

PY - 2012

Y1 - 2012

N2 - 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.

AB - 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.

U2 - 10.1016/j.bbamem.2012.04.003

DO - 10.1016/j.bbamem.2012.04.003

M3 - Journal article

C2 - 22525600

VL - 1818

SP - 2103

EP - 2107

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 9

ER -