Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression.
Protein Sci
; 24(10): 1695-701, 2015 Oct.
Article
em En
| MEDLINE
| ID: mdl-26174163
ABSTRACT
We recently reported the development of a computational method for the design of coassembling multicomponent protein nanomaterials. While four such materials were validated at high-resolution by X-ray crystallography, low yield of soluble protein prevented X-ray structure determination of a fifth designed material, T33-09. Here we report the design and crystal structure of T33-31, a variant of T33-09 with improved soluble yield resulting from redesign efforts focused on mutating solvent-exposed side chains to charged amino acids. The structure is found to match the computational design model with atomic-level accuracy, providing further validation of the design approach and demonstrating a simple and potentially general means of improving the yield of designed protein nanomaterials.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Variação Genética
/
Engenharia de Proteínas
/
Proteínas
/
Expressão Gênica
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article