4UOS

Thermodynamic hyperstability in parametrically designed helical bundles

4UOS の概要

• エントリーDOI: 10.2210/pdb4uos/pdb
• 関連するPDBエントリー: 4UOT
• 分子名称: DESIGNED HELICAL BUNDLE (2 entities in total)
• 機能のキーワード: de novo protein, protein design, thermodynamic hyperstability helical bundle
• 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: 22439.83

構造登録者

Oberdorfer, G.,Huang, P.,Pei, X.Y.,Xu, C.,Gonen, T.,Nannenga, B.,DiMaio, D.,Rogers, J.,Luisi, B.F.,Baker, D. (登録日: 2014-06-09, 公開日: 2014-11-05, 最終更新日: 2024-05-08)

主引用文献

Huang, P.,Oberdorfer, G.,Xu, C.,Pei, X.Y.,Nannenga, B.L.,Rogers, J.M.,Dimaio, F.,Gonen, T.,Luisi, B.,Baker, D.
High Thermodynamic Stability of Parametrically Designed Helical Bundles
Science, 346:481-, 2014

PubMed Abstract: We describe a procedure for designing proteins with backbones produced by varying the parameters in the Crick coiled coil-generating equations. Combinatorial design calculations identify low-energy sequences for alternative helix supercoil arrangements, and the helices in the lowest-energy arrangements are connected by loop building. We design an antiparallel monomeric untwisted three-helix bundle with 80-residue helices, an antiparallel monomeric right-handed four-helix bundle, and a pentameric parallel left-handed five-helix bundle. The designed proteins are extremely stable (extrapolated ΔGfold > 60 kilocalories per mole), and their crystal structures are close to those of the design models with nearly identical core packing between the helices. The approach enables the custom design of hyperstable proteins with fine-tuned geometries for a wide range of applications.

PubMed: 25342806
DOI: 10.1126/SCIENCE.1257481

実験手法

X-RAY DIFFRACTION (1.63 Å)