Computed structures of core eukaryotic protein complexes Journal Article


Authors: Humphreys, I.; Pei, J.; Baek, M.; Krishnakumar, A.; Anishchenko, I.; Ovchinnikov, S.; Zhang, J.; Ness, T. J.; Banjade, S.; Bagde, S. R.; Stancheva, V. G.; Li, X. H.; Liu, K.; Zheng, Z.; Barrero, D. J.; Roy, U.; Kuper, J.; Fernández, I. S.; Szakal, B.; Branzei, D.; Rizo, J.; Kisker, C.; Greene, E. C.; Biggins, S.; Keeney, S.; Miller, E. A.; Fromme, J. C.; Hendrickson, T. L.; Cong, Q.; Baker, D.
Article Title: Computed structures of core eukaryotic protein complexes
Abstract: Protein-protein interactions play critical roles in biology, but the structures of many eukaryotic protein complexes are unknown, and there are likely many interactions not yet identified. We take advantage of advances in proteome-wide amino acid coevolution analysis and deep-learning–based structure modeling to systematically identify and build accurate models of core eukaryotic protein complexes within the Saccharomyces cerevisiae proteome. We use a combination of RoseTTAFold and AlphaFold to screen through paired multiple sequence alignments for 8.3 million pairs of yeast proteins, identify 1505 likely to interact, and build structure models for 106 previously unidentified assemblies and 806 that have not been structurally characterized. These complexes, which have as many as five subunits, play roles in almost all key processes in eukaryotic cells and provide broad insights into biological function. © 2021 American Association for the Advancement of Science. All rights reserved.
Keywords: protein; amino acid; yeast; eukaryote; coevolution
Journal Title: Science
Volume: 374
Issue: 6573
ISSN: 0036-8075
Publisher: American Association for the Advancement of Science  
Date Published: 2021-12-10
Start Page: eabm4805
Language: English
DOI: 10.1126/science.abm4805
PROVIDER: scopus
PMCID: PMC7612107
PUBMED: 34762488
DOI/URL:
Notes: Article -- Export Date: 3 January 2022 -- Source: Scopus
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  1. Scott N Keeney
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  2. Kaixian Liu
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  3. Zhi Zheng
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