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Allosteric cooperation in a de novo-designed two-domain protein

Allosteric cooperation in a de novo-designed two-domain protein

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7776816

Allosteric cooperation in a de novo-designed two-domain protein

About this item

Full title

Allosteric cooperation in a de novo-designed two-domain protein

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2020-12, Vol.117 (52), p.33246-33253

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

We describe the de novo design of an allosterically regulated protein, which comprises two tightly coupled domains. One domain is based on the DF (Due Ferri in Italian or two-iron in English) family of de novo proteins, which have a diiron cofactor that catalyzes a phenol oxidase reaction, while the second domain is based on PS1 (Porphyrin-binding...

Alternative Titles

Full title

Allosteric cooperation in a de novo-designed two-domain protein

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7776816

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7776816

Other Identifiers

ISSN

0027-8424,1091-6490

E-ISSN

1091-6490

DOI

10.1073/pnas.2017062117

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