A de novo peptide hexamer with a mutable channel

The design of new proteins that expand the repertoire of natural protein structures represents a formidable challenge. Success in this area would increase understanding of protein structure, and present new scaffolds that could be exploited in biotechnology and synthetic biology. Here we describe th...

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Main Authors:	Zaccai, Nathan R., Chi, Bertie, Thomson, Andrew R., Boyle, Aimee L., Bartlett, Gail J., Bruning, Marc, Linden, Noah, Sessions, Richard B., Booth, Paula J., Brady, R. Leo, Woolfson, Derek N.
Format:	Online
Language:	English
Published:	2011
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3223406/

id	pubmed-3223406
recordtype	oai_dc
spelling	pubmed-32234062012-06-01 A de novo peptide hexamer with a mutable channel Zaccai, Nathan R. Chi, Bertie Thomson, Andrew R. Boyle, Aimee L. Bartlett, Gail J. Bruning, Marc Linden, Noah Sessions, Richard B. Booth, Paula J. Brady, R. Leo Woolfson, Derek N. Article The design of new proteins that expand the repertoire of natural protein structures represents a formidable challenge. Success in this area would increase understanding of protein structure, and present new scaffolds that could be exploited in biotechnology and synthetic biology. Here we describe the design, characterisation and X-ray crystal structure of a new coiled-coil protein. The de novo sequence forms a stand-alone, parallel, 6-helix bundle with a channel running through it. Although lined exclusively by hydrophobic leucine and isoleucine side chains, the 6 Å channel is permeable to water. One layer of leucine residues within the channel is mutable accepting polar aspartic acid (Asp) and histidine (His) side chains, and leading to subdivision and organization of solvent within the lumen. Moreover, these mutants can be combined to form a stable and unique (Asp-His)3 heterohexamer. These new structures provide a basis for engineering de novo proteins with new functions. 2011-10-30 /pmc/articles/PMC3223406/ /pubmed/22037471 http://dx.doi.org/10.1038/nchembio.692 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Zaccai, Nathan R. Chi, Bertie Thomson, Andrew R. Boyle, Aimee L. Bartlett, Gail J. Bruning, Marc Linden, Noah Sessions, Richard B. Booth, Paula J. Brady, R. Leo Woolfson, Derek N.
spellingShingle	Zaccai, Nathan R. Chi, Bertie Thomson, Andrew R. Boyle, Aimee L. Bartlett, Gail J. Bruning, Marc Linden, Noah Sessions, Richard B. Booth, Paula J. Brady, R. Leo Woolfson, Derek N. A de novo peptide hexamer with a mutable channel
author_facet	Zaccai, Nathan R. Chi, Bertie Thomson, Andrew R. Boyle, Aimee L. Bartlett, Gail J. Bruning, Marc Linden, Noah Sessions, Richard B. Booth, Paula J. Brady, R. Leo Woolfson, Derek N.
author_sort	Zaccai, Nathan R.
title	A de novo peptide hexamer with a mutable channel
title_short	A de novo peptide hexamer with a mutable channel
title_full	A de novo peptide hexamer with a mutable channel
title_fullStr	A de novo peptide hexamer with a mutable channel
title_full_unstemmed	A de novo peptide hexamer with a mutable channel
title_sort	de novo peptide hexamer with a mutable channel
description	The design of new proteins that expand the repertoire of natural protein structures represents a formidable challenge. Success in this area would increase understanding of protein structure, and present new scaffolds that could be exploited in biotechnology and synthetic biology. Here we describe the design, characterisation and X-ray crystal structure of a new coiled-coil protein. The de novo sequence forms a stand-alone, parallel, 6-helix bundle with a channel running through it. Although lined exclusively by hydrophobic leucine and isoleucine side chains, the 6 Å channel is permeable to water. One layer of leucine residues within the channel is mutable accepting polar aspartic acid (Asp) and histidine (His) side chains, and leading to subdivision and organization of solvent within the lumen. Moreover, these mutants can be combined to form a stable and unique (Asp-His)3 heterohexamer. These new structures provide a basis for engineering de novo proteins with new functions.
publishDate	2011
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3223406/
_version_	1611489820999155712

A de novo peptide hexamer with a mutable channel

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