Redox- and metal-directed structural diversification in designed metalloprotein assemblies

Albert Kakkis; Eyal Golub; Tae Su Choi; F. Akif Tezcan

doi:10.1039/d2cc02440c

Redox- and metal-directed structural diversification in designed metalloprotein assemblies

Albert Kakkis, Eyal Golub, Tae Su Choi, F. Akif Tezcan

University of California at San Diego

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

Herein we describe a designed protein building block whose self-assembly behaviour is dually gated by the redox state of disulphide bonds and the identity of exogenous metal ions. This protein construct is shown - through extensive structural and biophysical characterization - to access five distinct oligomeric states, exemplifying how the complex interplay between hydrophobic, metal-ligand, and reversible covalent interactions could be harnessed to obtain multiple, responsive protein architectures from a single building block.

Original language	English
Pages (from-to)	6958-6961
Number of pages	4
Journal	Chemical Communications
Volume	58
Issue number	49
DOIs	https://doi.org/10.1039/d2cc02440c
State	Published - 16 Jun 2022
Externally published	Yes

Bibliographical note

Publisher Copyright:
© 2022 The Royal Society of Chemistry

Funding

Funders	Funder number
National Institute of General Medical Sciences	P30GM133894

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10.1039/d2cc02440c

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Redox- and metal-directed structural diversification in designed metalloprotein assemblies

Abstract

Bibliographical note

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