7BIM

A de novo designed nonameric coiled coil, CC-Type2-(GgLaId)4

7BIM の概要

• エントリーDOI: 10.2210/pdb7bim/pdb
• 関連するPDBエントリー: 7A1T 7BAS 7BAT 7BAU 7BAV 7BAW
• 分子名称: Nonameric de novo coiled coil CC-Type2-(GgLaId)4, GLYCEROL, ISOPROPYL ALCOHOL, ... (4 entities in total)
• 機能のキーワード: coiled coil, alpha-helical barrel, nonamer, synthetic, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 36
• 化学式量合計: 118447.94

構造登録者

Shelley, K.L.,Rhys, G.G.,Dawson, W.M.,Brady, R.L.,Woolfson, D.N. (登録日: 2021-01-12, 公開日: 2021-04-21, 最終更新日: 2024-10-23)

主引用文献

Dawson, W.M.,Martin, F.J.O.,Rhys, G.G.,Shelley, K.L.,Brady, R.L.,Woolfson, D.N.
Coiled coils 9-to-5: rational de novo design of alpha-helical barrels with tunable oligomeric states.
Chem Sci, 12:6923-6928, 2021

PubMed Abstract: The rational design of linear peptides that assemble controllably and predictably in water is challenging. Short sequences must encode unique target structures and avoid alternative states. However, the non-covalent forces that stabilize and discriminate between states are weak. Nonetheless, for α-helical coiled-coil assemblies considerable progress has been made in rational design. In these, sequence repeats of nominally hydrophobic () and polar () residues, , direct the assembly of amphipathic helices into dimeric to tetrameric bundles. Expanding this pattern to can produce larger α-helical barrels. Here, we show that pentameric to nonameric barrels are accessed by varying the residue at one of the sites. In peptides with four L/I-K-E-I-A-x-Z repeats, decreasing the size of Z from threonine to serine to alanine to glycine gives progressively larger oligomers. X-ray crystal structures of the resulting α-helical barrels rationalize this: side chains at Z point directly into the helical interfaces, and smaller residues allow closer helix contacts and larger assemblies.

PubMed: 34745518
DOI: 10.1039/d1sc00460c

実験手法

X-RAY DIFFRACTION (1.64 Å)