2HKD

The crystal structure of engineered OSPA

2HKD の概要

• エントリーDOI: 10.2210/pdb2hkd/pdb
• 分子名称: Outer Surface Protein A, TETRAETHYLENE GLYCOL (3 entities in total)
• 機能のキーワード: beta sheet, engineered protein, de novo protein
• 由来する生物種: Borreliella burgdorferi (Lyme disease spirochete)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34576.43

構造登録者

Makabe, K.,Terechko, V.,Koide, S. (登録日: 2006-07-03, 公開日: 2006-11-21, 最終更新日: 2023-08-30)

主引用文献

Makabe, K.,McElheny, D.,Tereshko, V.,Hilyard, A.,Gawlak, G.,Yan, S.,Koide, A.,Koide, S.
Atomic structures of peptide self-assembly mimics.
Proc.Natl.Acad.Sci.Usa, 103:17753-17758, 2006

PubMed Abstract: Although the beta-rich self-assemblies are a major structural class for polypeptides and the focus of intense research, little is known about their atomic structures and dynamics due to their insoluble and noncrystalline nature. We developed a protein engineering strategy that captures a self-assembly segment in a water-soluble molecule. A predefined number of self-assembling peptide units are linked, and the beta-sheet ends are capped to prevent aggregation, which yields a mono-dispersed soluble protein. We tested this strategy by using Borrelia outer surface protein (OspA) whose single-layer beta-sheet located between two globular domains consists of two beta-hairpin units and thus can be considered as a prototype of self-assembly. We constructed self-assembly mimics of different sizes and determined their atomic structures using x-ray crystallography and NMR spectroscopy. Highly regular beta-sheet geometries were maintained in these structures, and peptide units had a nearly identical conformation, supporting the concept that a peptide in the regular beta-geometry is primed for self-assembly. However, we found small but significant differences in the relative orientation between adjacent peptide units in terms of beta-sheet twist and bend, suggesting their inherent flexibility. Modeling shows how this conformational diversity, when propagated over a large number of peptide units, can lead to a substantial degree of nanoscale polymorphism of self-assemblies.

PubMed: 17093048
DOI: 10.1073/pnas.0606690103

実験手法

X-RAY DIFFRACTION (1.6 Å)