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Coevolutionary constraints in the sequence‐space of macromolecular complexes reflect their self‐assembly pathways
Author(s) -
Mallik Saurav,
Kundu Sudip
Publication year - 2017
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25292
Subject(s) - macromolecule , sequence (biology) , complementarity (molecular biology) , monomer , sequence space , hierarchy , coevolution , self assembly , stoichiometry , computer science , chemistry , computational biology , biology , evolutionary biology , nanotechnology , materials science , mathematics , genetics , polymer , organic chemistry , economics , pure mathematics , banach space , market economy
ABSTRACT Is the order in which biomolecular subunits self‐assemble into functional macromolecular complexes imprinted in their sequence‐space? Here, we demonstrate that the temporal order of macromolecular complex self‐assembly can be efficiently captured using the landscape of residue‐level coevolutionary constraints. This predictive power of coevolutionary constraints is irrespective of the structural, functional, and phylogenetic classification of the complex and of the stoichiometry and quaternary arrangement of the constituent monomers. Combining this result with a number of structural attributes estimated from the crystal structure data, we find indications that stronger coevolutionary constraints at interfaces formed early in the assembly hierarchy probably promotes coordinated fixation of mutations that leads to high‐affinity binding with higher surface area, increased surface complementarity and elevated number of molecular contacts, compared to those that form late in the assembly. Proteins 2017; 85:1183–1189. © 2017 Wiley Periodicals, Inc.