1SWI

GCN4-LEUCINE ZIPPER CORE MUTANT AS N16A COMPLEXED WITH BENZENE

1SWI の概要

• エントリーDOI: 10.2210/pdb1swi/pdb
• 分子名称: GCN4P1, BENZENE (3 entities in total)
• 機能のキーワード: coiled coil, leucine zipper
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 11966.03

構造登録者

Gonzalez, L.,Plecs, J.,Alber, T. (登録日: 1996-05-09, 公開日: 1996-11-08, 最終更新日: 2024-02-14)

主引用文献

Gonzalez Jr., L.,Plecs, J.J.,Alber, T.
An engineered allosteric switch in leucine-zipper oligomerization.
Nat.Struct.Biol., 3:510-515, 1996

PubMed Abstract: Controversy remains about the role of core side-chain packing in specifying protein structure. To investigate the influence of core packing on the oligomeric structure of a coiled coil, we engineered a GCN4 leucine zipper mutant that switches from two to three strands upon binding the hydrophobic ligands cyclohexane and benzene. In solution these ligands increased the apparent thermal stability and the oligomerization order of the mutant leucine zipper. The crystal structure of the peptide-benzene complex shows a single benzene molecule bound at the engineered site in the core of the trimer. These results indicate that coiled coils are well-suited to function as molecular switches and emphasize that core packing is an important determinant of oligomerization specificity.

PubMed: 8646536
DOI: 10.1038/nsb0696-510

実験手法

X-RAY DIFFRACTION (2.6 Å)