1BB1

CRYSTAL STRUCTURE OF A DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL

1BB1 の概要

• エントリーDOI: 10.2210/pdb1bb1/pdb
• 分子名称: DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: de novo protein design, coiled coil
• 由来する生物種: synthetic construct; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 11246.58

構造登録者

Nautiyal, S.,Alber, T. (登録日: 1998-04-28, 公開日: 1999-02-02, 最終更新日: 2024-10-16)

主引用文献

Nautiyal, S.,Alber, T.
Crystal structure of a designed, thermostable, heterotrimeric coiled coil.
Protein Sci., 8:84-90, 1999

PubMed Abstract: Electrostatic interactions are often critical for determining the specificity of protein-protein complexes. To study the role of electrostatic interactions for assembly of helical bundles, we previously designed a thermostable, heterotrimeric coiled coil, ABC, in which charged residues were employed to drive preferential association of three distinct, 34-residue helices. To investigate the basis for heterotrimer specificity, we have used multiwavelength anomalous diffraction (MAD) analysis to determine the 1.8 A resolution crystal structure of ABC. The structure shows that ABC forms a heterotrimeric coiled coil with the intended arrangement of parallel chains. Over half of the ion pairs engineered to restrict helix associations were apparent in the experimental electron density map. As seen in other trimeric coiled coils, ABC displays acute knobs-into-holes packing and a buried anion coordinated by core polar amino acids. These interactions validate the design strategy and illustrate how packing and polar contacts determine structural uniqueness.

PubMed: 10210186

実験手法

X-RAY DIFFRACTION (1.8 Å)