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

Mathias Weber; Lydia Tome; Daniel Otzen; Dirk Schneider

doi:10.1016/j.bbamem.2012.04.003

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

Mathias Weber, Lydia Tome, Daniel Otzen, Dirk Schneider

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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.

Original language	English
Journal	BBA General Subjects
Volume	1818
Issue	9
Pages (from-to)	2103-7
Number of pages	5
ISSN	0304-4165
DOIs	https://doi.org/10.1016/j.bbamem.2012.04.003
Publication status	Published - 2012

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10.1016/j.bbamem.2012.04.003

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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",

year = "2012",

doi = "10.1016/j.bbamem.2012.04.003",

language = "English",

volume = "1818",

pages = "2103--7",

journal = "BBA General Subjects",

issn = "0304-4165",

publisher = "Elsevier BV",

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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

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

SN - 0304-4165

VL - 1818

SP - 2103

EP - 2107

JO - BBA General Subjects

JF - BBA General Subjects

IS - 9

ER -

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

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