6FF6

Crystal structure of novel repeat protein BRIC1

6FF6 の概要

• エントリーDOI: 10.2210/pdb6ff6/pdb
• 分子名称: BRIC1 (1 entity in total)
• 機能のキーワード: novel fold, computational design, corrugated repeat, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28491.47

構造登録者

ElGamacy, M.,Coles, M.,Ernst, P.,Zhu, H.,Hartmann, M.D.,Plueckthun, A.,Lupas, A.N. (登録日: 2018-01-03, 公開日: 2018-09-05, 最終更新日: 2024-05-08)

主引用文献

ElGamacy, M.,Coles, M.,Ernst, P.,Zhu, H.,Hartmann, M.D.,Pluckthun, A.,Lupas, A.N.
An Interface-Driven Design Strategy Yields a Novel, Corrugated Protein Architecture.
ACS Synth Biol, 7:2226-2235, 2018

PubMed Abstract: Designing proteins with novel folds remains a major challenge, as the biophysical properties of the target fold are not known a priori and no sequence profile exists to describe its features. Therefore, most computational design efforts so far have been directed toward creating proteins that recapitulate existing folds. Here we present a strategy centered upon the design of novel intramolecular interfaces that enables the construction of a target fold from a set of starting fragments. This strategy effectively reduces the amount of computational sampling necessary to achieve an optimal sequence, without compromising the level of topological control. The solenoid architecture has been a target of extensive protein design efforts, as it provides a highly modular platform of low topological complexity. However, none of the previous efforts have attempted to depart from the natural form, which is characterized by a uniformly handed superhelical architecture. Here we aimed to design a more complex platform, abolishing the superhelicity by introducing internally alternating handedness, resulting in a novel, corrugated architecture. We employed our interface-driven strategy, designing three proteins and confirming the design by solving the structure of two examples.

PubMed: 30148951
DOI: 10.1021/acssynbio.8b00224

実験手法

X-RAY DIFFRACTION (2.5 Å)