A Completely de Novo ATPase from Combinatorial Protein Design

Michael S. Wang; Michael H. Hecht

doi:10.1021/jacs.0c02954

A Completely de Novo ATPase from Combinatorial Protein Design

Michael S. Wang, Michael H. Hecht

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

7 Scopus citations

Abstract

Our understanding of biological chemistry is shaped by the observation that all life comes from other life - as Pasteur put it, omne vivum ex vivo. A key step in expanding our biochemical vocabulary is to recapitulate biogenic catalysis using non-natural sequences that did not arise from common ancestry. Here we describe an enzyme designed completely de novo that hydrolyzes ATP. This protein was designed to lack β-sheet structure and is competitively inhibited by magnesium, two traits that are unlike natural ATPases.

Original language	English (US)
Pages (from-to)	15230-15234
Number of pages	5
Journal	Journal of the American Chemical Society
Volume	142
Issue number	36
DOIs	https://doi.org/10.1021/jacs.0c02954
State	Published - Sep 9 2020

All Science Journal Classification (ASJC) codes

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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abstract = "Our understanding of biological chemistry is shaped by the observation that all life comes from other life - as Pasteur put it, omne vivum ex vivo. A key step in expanding our biochemical vocabulary is to recapitulate biogenic catalysis using non-natural sequences that did not arise from common ancestry. Here we describe an enzyme designed completely de novo that hydrolyzes ATP. This protein was designed to lack β-sheet structure and is competitively inhibited by magnesium, two traits that are unlike natural ATPases. ",

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note = "Funding Information: We thank Venu Vandavasi for assistance with AUC, Kaelix Johnson for assistance making some constructs, and Shlomo Zarzhitsky for helpful feedback throughout. This work was supported by NSF grants MCB-1409402 and MCB-1947720. Publisher Copyright: {\textcopyright} 2020 American Chemical Society.",

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A Completely de Novo ATPase from Combinatorial Protein Design

Abstract

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