Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression
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.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Aug 06, 2015
- Source ID
- 10.1002/pro.2748
Entities
People
- David Baker
- Duilio Cascio
- Jacob B. Bale
- Neil P. King
- Rachel U. Park
- Shane Gonen
- Tamir Gonen
- Todd O. Yeates
- Yuxi Liu
Organizations
- Defense Advanced Research Projects Agency
- Howard Hughes Medical Institute
- National Science Foundation
- University of California, Los Angeles
- University of Washington