Large scale determination of previously unsolved protein structures using evolutionary information
- University of Washington, United States
- Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, United States
- University of Texas Southwestern Medical Center, United States
- Facebook Inc., United States
Abstract
The prediction of the structures of proteins without detectablesequence similarity to any protein of known structure remains anoutstanding scientific challenge. Here we describe de novo blindstructure predictions of unprecedented accuracy for two proteins in large families made in the recent CASP11 blind test of protein structure prediction methods by incorporating residue-residue co-evolution information in the Rosetta structure prediction program. We then use the method to generate structure models for 58 of the 121 large protein families in prokaryotes for which three dimensionalstructures are not available. These models, which are posted online for public access, provide structural information for the over 400,000 proteins belonging to the 58 families and suggest hypotheses about mechanism for the subset for which the function is known, and hypotheses about function for the remainder.
Article and author information
Author details
Reviewing Editor
- Yibing Shan, DE Shaw Research, United States
Version history
- Received: June 6, 2015
- Accepted: August 30, 2015
- Accepted Manuscript published: September 3, 2015 (version 1)
- Version of Record published: October 21, 2015 (version 2)
Copyright
© 2015, Ovchinnikov et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Large scale determination of previously unsolved protein structures using evolutionary information
eLife 4:e09248.
https://doi.org/10.7554/eLife.09248
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