5DQA

t3284 loop variant of beta1

5DQA の概要

• エントリーDOI: 10.2210/pdb5dqa/pdb
• 分子名称: t3284 (1 entity in total)
• 機能のキーワード: synthetic protein, loop design, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 76505.61

構造登録者

Kabasakal, B.V.,MacDonald, J.T.,Murray, W.W. (登録日: 2015-09-14, 公開日: 2016-08-31, 最終更新日: 2024-05-08)

主引用文献

MacDonald, J.T.,Kabasakal, B.V.,Godding, D.,Kraatz, S.,Henderson, L.,Barber, J.,Freemont, P.S.,Murray, J.W.
Synthetic beta-solenoid proteins with the fragment-free computational design of a beta-hairpin extension.
Proc.Natl.Acad.Sci.USA, 113:10346-10351, 2016

PubMed Abstract: The ability to design and construct structures with atomic level precision is one of the key goals of nanotechnology. Proteins offer an attractive target for atomic design because they can be synthesized chemically or biologically and can self-assemble. However, the generalized protein folding and design problem is unsolved. One approach to simplifying the problem is to use a repetitive protein as a scaffold. Repeat proteins are intrinsically modular, and their folding and structures are better understood than large globular domains. Here, we have developed a class of synthetic repeat proteins based on the pentapeptide repeat family of beta-solenoid proteins. We have constructed length variants of the basic scaffold and computationally designed de novo loops projecting from the scaffold core. The experimentally solved 3.56-Å resolution crystal structure of one designed loop matches closely the designed hairpin structure, showing the computational design of a backbone extension onto a synthetic protein core without the use of backbone fragments from known structures. Two other loop designs were not clearly resolved in the crystal structures, and one loop appeared to be in an incorrect conformation. We have also shown that the repeat unit can accommodate whole-domain insertions by inserting a domain into one of the designed loops.

PubMed: 27573845
DOI: 10.1073/pnas.1525308113

実験手法

X-RAY DIFFRACTION (3.27 Å)