Open AccessAllosteric cooperation in a de novo-designed two-domain protein
Author(s) -
Fabio Pirro,
Nathan W. Schmidt,
James Lincoff,
Zachary Widel,
Nicholas F. Polizzi,
Lijun Liu,
Michael J. Therien,
Michael Grabe,
Marco Chino,
Angela Lombardi,
William F. DeGrado
Publication year - 2020
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2017062117
Subject(s) - allosteric regulation , computational biology , encode , domain (mathematical analysis) , protein design , chemistry , enzyme , protein structure , gene , biochemistry , biology , mathematical analysis , mathematics
Significance A major mechanism of evolution involves fusing genes that encode single-domain proteins to create multidomain structures that achieve new functions. Here, we develop methods to design multidomain proteins entirely from scratch and achieve the premier de novo design of an allosterically regulated phenol oxidase that responds to the binding of a synthetic porphyrin.