1XOF

Heterooligomeric Beta Beta Alpha Miniprotein

Summary for 1XOF

• Entry DOI: 10.2210/pdb1xof/pdb
• Related: 1SN9 1SNA 1SNE
• Descriptor: BBAhetT1 (3 entities in total)
• Functional Keywords: protein design, heterooligomer, heterotetramer, de novo protein
• Total number of polymer chains: 2
• Total formula weight: 5187.89

Authors

Ali, M.H.,Taylor, C.M.,Grigoryan, G.,Allen, K.N.,Imperiali, B.,Keating, A.E. (deposition date: 2004-10-06, release date: 2005-02-01, Last modification date: 2023-11-15)

Primary citation

Ali, M.H.,Taylor, C.M.,Grigoryan, G.,Allen, K.N.,Imperiali, B.,Keating, A.E.
Design of a Heterospecific, Tetrameric, 21-Residue Miniprotein with Mixed alpha/beta Structure.
Structure, 13:225-234, 2005

PubMed Abstract: The study of short, autonomously folding peptides, or "miniproteins," is important for advancing our understanding of protein stability and folding specificity. Although many examples of synthetic alpha-helical structures are known, relatively few mixed alpha/beta structures have been successfully designed. Only one mixed-secondary structure oligomer, an alpha/beta homotetramer, has been reported thus far. In this report, we use structural analysis and computational design to convert this homotetramer into the smallest known alpha/beta-heterotetramer. Computational screening of many possible sequence/structure combinations led efficiently to the design of short, 21-residue peptides that fold cooperatively and autonomously into a specific complex in solution. A 1.95 A crystal structure reveals how steric complementarity and charge patterning encode heterospecificity. The first- and second-generation heterotetrameric miniproteins described here will be useful as simple models for the analysis of protein-protein interaction specificity and as structural platforms for the further elaboration of folding and function.

PubMed: 15698566
DOI: 10.1016/j.str.2004.12.009

Experimental method

X-RAY DIFFRACTION (1.95 Å)