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Computed structures of core eukaryotic protein complexes.

Authors :
Humphreys IR
Pei J
Baek M
Krishnakumar A
Anishchenko I
Ovchinnikov S
Zhang J
Ness TJ
Banjade S
Bagde SR
Stancheva VG
Li XH
Liu K
Zheng Z
Barrero DJ
Roy U
Kuper J
Fernández IS
Szakal B
Branzei D
Rizo J
Kisker C
Greene EC
Biggins S
Keeney S
Miller EA
Fromme JC
Hendrickson TL
Cong Q
Baker D
Source :
Science (New York, N.Y.) [Science] 2021 Dec 10; Vol. 374 (6573), pp. eabm4805. Date of Electronic Publication: 2021 Dec 10.
Publication Year :
2021

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.

Details

Language :
English
ISSN :
1095-9203
Volume :
374
Issue :
6573
Database :
MEDLINE
Journal :
Science (New York, N.Y.)
Publication Type :
Academic Journal
Accession number :
34762488
Full Text :
https://doi.org/10.1126/science.abm4805