3AUM

Crystal structure of OspA mutant

3AUM の概要

• エントリーDOI: 10.2210/pdb3aum/pdb
• 分子名称: Outer surface protein A (2 entities in total)
• 機能のキーワード: beta-mender, membrane protein
• 由来する生物種: Borrelia burgdorferi (Lyme disease spirochete)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26939.00

構造登録者

Makabe, K. (登録日: 2011-02-10, 公開日: 2012-02-15, 最終更新日: 2023-11-01)

主引用文献

Biancalana, M.,Makabe, K.,Yan, S.,Koide, S.
Aromatic cluster mutations produce focal modulations of beta-sheet structure.
Protein Sci., 24:841-849, 2015

PubMed Abstract: Site-directed mutagenesis is a powerful tool for altering the structure and function of proteins in a focused manner. Here, we examined how a model β-sheet protein could be tuned by mutation of numerous surface-exposed residues to aromatic amino acids. We designed these aromatic side chain "clusters" at highly solvent-exposed positions in the flat, single-layer β-sheet of Borrelia outer surface protein A (OspA). This unusual β-sheet scaffold allows us to interrogate the effects of these mutations in the context of well-defined structure but in the absence of the strong scaffolding effects of globular protein architecture. We anticipated that the introduction of a cluster of aromatic amino acid residues on the β-sheet surface would result in large conformational changes and/or stabilization and thereby provide new means of controlling the properties of β-sheets. Surprisingly, X-ray crystal structures revealed that the introduction of aromatic clusters produced only subtle conformational changes in the OspA β-sheet. Additionally, despite burying a large degree of hydrophobic surface area, the aromatic cluster mutants were slightly less stable than the wild-type scaffold. These results thereby demonstrate that the introduction of aromatic cluster mutations can serve as a means for subtly modulating β-sheet conformation in protein design.

PubMed: 25645104
DOI: 10.1002/pro.2657

実験手法

X-RAY DIFFRACTION (1.6 Å)