α/β coiled coils

ELife
Marcus D HartmannBirte Hernandez Alvarez

Abstract

Coiled coils are the best-understood protein fold, as their backbone structure can uniquely be described by parametric equations. This level of understanding has allowed their manipulation in unprecedented detail. They do not seem a likely source of surprises, yet we describe here the unexpected formation of a new type of fiber by the simple insertion of two or six residues into the underlying heptad repeat of a parallel, trimeric coiled coil. These insertions strain the supercoil to the breaking point, causing the local formation of short β-strands, which move the path of the chain by 120° around the trimer axis. The result is an α/β coiled coil, which retains only one backbone hydrogen bond per repeat unit from the parent coiled coil. Our results show that a substantially novel backbone structure is possible within the allowed regions of the Ramachandran space with only minor mutations to a known fold.

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Citations

Aug 6, 2016·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·Linda Truebestein, Thomas A Leonard
Sep 29, 2020·The Journal of Biological Chemistry·Aaron C Mason, Susan R Wente
Dec 17, 2020·Bioinformatics·Krzysztof SzczepaniakStanislaw Dunin-Horkawicz
Jan 18, 2021·The Journal of Biological Chemistry·Aaron C Mason, Susan R Wente
May 9, 2021·Current Opinion in Structural Biology·Mohammad ElGamacy, Birte Hernandez Alvarez
Aug 25, 2021·Prion·Molood BehbahanipourSalvador Ventura

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Datasets Mentioned

BETA
SF370.1

Software Mentioned

MOLREP
HHblits
Raster3D
PatternSearch
REFMAC5
HHpred
MolScript
WebLogo3
PSI
HMMER

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