3R4A

Crystal structure of the 4-helix coiled coil CC-tet

3R4A の概要

• エントリーDOI: 10.2210/pdb3r4a/pdb
• 関連するPDBエントリー: 3R4H
• 分子名称: coiled coil helix CC-tet (2 entities in total)
• 機能のキーワード: coiled coil domain, tetramer, kih interactions, synthetic biology, de novo protein
• 由来する生物種: Synthetic construct
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 13452.00

構造登録者

Zaccai, N.R.,Chi, B.H.C.,Woolfson, D.N.,Brady, R.L. (登録日: 2011-03-17, 公開日: 2011-11-16, 最終更新日: 2024-11-06)

主引用文献

Zaccai, N.R.,Chi, B.,Thomson, A.R.,Boyle, A.L.,Bartlett, G.J.,Bruning, M.,Linden, N.,Sessions, R.B.,Booth, P.J.,Brady, R.L.,Woolfson, D.N.
A de novo peptide hexamer with a mutable channel.
Nat.Chem.Biol., 7:935-941, 2011

PubMed Abstract: The design of new proteins that expand the repertoire of natural protein structures represents a formidable challenge. Success in this area would increase understanding of protein structure and present new scaffolds that could be exploited in biotechnology and synthetic biology. Here we describe the design, characterization and X-ray crystal structure of a new coiled-coil protein. The de novo sequence forms a stand-alone, parallel, six-helix bundle with a channel running through it. Although lined exclusively by hydrophobic leucine and isoleucine side chains, the 6-Å channel is permeable to water. One layer of leucine residues within the channel is mutable, accepting polar aspartic acid and histidine side chains, which leads to subdivision and organization of solvent within the lumen. Moreover, these mutants can be combined to form a stable and unique (Asp-His)(3) heterohexamer. These new structures provide a basis for engineering de novo proteins with new functions.

PubMed: 22037471
DOI: 10.1038/nchembio.692

実験手法

X-RAY DIFFRACTION (2.0701 Å)