Structure and stability of the designer protein WRAP-T and its permutants

Abstract $$\beta $$ β -Propeller proteins are common natural disc-like pseudo-symmetric proteins that contain multiple repeats (‘blades’) each consisting of a 4-stranded anti-parallel $$\beta $$ β -sheet. So far, 4- to 12-bladed $$\beta $$ β -propellers have been discovered in nature showing large f...

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Autores principales:	Bram Mylemans, Xiao Yin Lee, Ina Laier, Christine Helsen, Arnout R. D. Voet
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/4f79e968ad0342daa7075fc81ab3f3d7
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spelling	oai:doaj.org-article:4f79e968ad0342daa7075fc81ab3f3d72021-12-02T15:15:23ZStructure and stability of the designer protein WRAP-T and its permutants10.1038/s41598-021-98391-02045-2322https://doaj.org/article/4f79e968ad0342daa7075fc81ab3f3d72021-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-98391-0https://doaj.org/toc/2045-2322Abstract $$\beta $$ β -Propeller proteins are common natural disc-like pseudo-symmetric proteins that contain multiple repeats (‘blades’) each consisting of a 4-stranded anti-parallel $$\beta $$ β -sheet. So far, 4- to 12-bladed $$\beta $$ β -propellers have been discovered in nature showing large functional and sequential variation. Using computational design approaches, we created perfectly symmetric $$\beta $$ β -propellers out of natural pseudo-symmetric templates. These proteins are useful tools to study protein evolution of this very diverse fold. While the 7-bladed architecture is the most common, no symmetric 7-bladed monomer has been created and characterized so far. Here we describe such a engineered protein, based on a highly symmetric natural template, and test the effects of circular permutation on its stability. Geometrical analysis of this protein and other artificial symmetrical proteins reveals no systematic constraint that could be used to help in engineering of this fold, and suggests sequence constraints unique to each $$\beta $$ β -propeller sub-family.Bram MylemansXiao Yin LeeIna LaierChristine HelsenArnout R. D. VoetNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Bram Mylemans Xiao Yin Lee Ina Laier Christine Helsen Arnout R. D. Voet Structure and stability of the designer protein WRAP-T and its permutants
description	Abstract $$\beta $$ β -Propeller proteins are common natural disc-like pseudo-symmetric proteins that contain multiple repeats (‘blades’) each consisting of a 4-stranded anti-parallel $$\beta $$ β -sheet. So far, 4- to 12-bladed $$\beta $$ β -propellers have been discovered in nature showing large functional and sequential variation. Using computational design approaches, we created perfectly symmetric $$\beta $$ β -propellers out of natural pseudo-symmetric templates. These proteins are useful tools to study protein evolution of this very diverse fold. While the 7-bladed architecture is the most common, no symmetric 7-bladed monomer has been created and characterized so far. Here we describe such a engineered protein, based on a highly symmetric natural template, and test the effects of circular permutation on its stability. Geometrical analysis of this protein and other artificial symmetrical proteins reveals no systematic constraint that could be used to help in engineering of this fold, and suggests sequence constraints unique to each $$\beta $$ β -propeller sub-family.
format	article
author	Bram Mylemans Xiao Yin Lee Ina Laier Christine Helsen Arnout R. D. Voet
author_facet	Bram Mylemans Xiao Yin Lee Ina Laier Christine Helsen Arnout R. D. Voet
author_sort	Bram Mylemans
title	Structure and stability of the designer protein WRAP-T and its permutants
title_short	Structure and stability of the designer protein WRAP-T and its permutants
title_full	Structure and stability of the designer protein WRAP-T and its permutants
title_fullStr	Structure and stability of the designer protein WRAP-T and its permutants
title_full_unstemmed	Structure and stability of the designer protein WRAP-T and its permutants
title_sort	structure and stability of the designer protein wrap-t and its permutants
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/4f79e968ad0342daa7075fc81ab3f3d7
work_keys_str_mv	AT brammylemans structureandstabilityofthedesignerproteinwraptanditspermutants AT xiaoyinlee structureandstabilityofthedesignerproteinwraptanditspermutants AT inalaier structureandstabilityofthedesignerproteinwraptanditspermutants AT christinehelsen structureandstabilityofthedesignerproteinwraptanditspermutants AT arnoutrdvoet structureandstabilityofthedesignerproteinwraptanditspermutants
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Structure and stability of the designer protein WRAP-T and its permutants

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