4ZK7

Crystal structure of rescued two-component self-assembling tetrahedral cage T33-31

Summary for 4ZK7

• Entry DOI: 10.2210/pdb4zk7/pdb
• Descriptor: Chorismate mutase, Divalent-cation tolerance protein CutA (2 entities in total)
• Functional Keywords: tetrahedral, computational design, rosetta, self-assembly, symmetric, nanomaterial, solubility, protein binding
• Biological source: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); More
• Cellular location: Cytoplasm : Q5SJY4 Q7SIA8
• Total number of polymer chains: 24
• Total formula weight: 324480.56

Authors

Liu, Y.,Cascio, D.,Sawaya, M.R.,Bale, J.,Collazo, M.J.,Park, R.,King, N.,Baker, D.,Yeates, T. (deposition date: 2015-04-30, release date: 2015-07-29, Last modification date: 2024-03-06)

Primary citation

Bale, J.B.,Park, R.U.,Liu, Y.,Gonen, S.,Gonen, T.,Cascio, D.,King, N.P.,Yeates, T.O.,Baker, D.
Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression.
Protein Sci., 24:1695-1701, 2015

PubMed 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.

PubMed: 26174163
DOI: 10.1002/pro.2748

Experimental method

X-RAY DIFFRACTION (3.4 Å)