6LJY

A Crystal Structure of OspA mutant

6LJY の概要

• エントリーDOI: 10.2210/pdb6ljy/pdb
• 分子名称: OspA163 (2 entities in total)
• 機能のキーワード: outer surface protein a, ospa, lipid binding protein
• 由来する生物種: Borreliella burgdorferi
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25416.32

構造登録者

Kiya, M.,Makabe, K. (登録日: 2019-12-17, 公開日: 2020-12-23, 最終更新日: 2024-02-21)

主引用文献

Kiya, M.,Shiga, S.,Ding, P.,Koide, S.,Makabe, K.
beta-Strand-mediated Domain-swapping in the Absence of Hydrophobic Core Repacking.
J.Mol.Biol., 436:168405-168405, 2024

PubMed Abstract: Domain swapping is a process wherein a portion of a protein is exchanged with its counterpart in another copy of the molecule, resulting in the formation of homo-oligomers with concomitant repacking of a hydrophobic core. Here, we report domain swapping triggered upon modifying a β-hairpin sequence within a single-layer β-sheet (SLB) of a model protein, OspA that did not involve the formation of a reorganized hydrophobic core. The replacement of two β-hairpin sequences with a Gly-Gly and shorteing of a β-hairpin resulted in a protein that formed two distinct crystal structures under similar conditions: one was monomeric, similar to the parental molecule, whereas the other was a domain-swapped dimer, mediated by an intermolecular β-sheet in the SLB portion. Based on the dimer interface structure, we replaced the Gly-Gly sequence with three-residue sequences that enable the formation of a consecutive intermolecular β-sheet, including the Cys-Thr-Cys sequence that formed a stable disulfide-linked dimer. These results provide new insights into protein folding, evolution, and the designability of protein structure.

PubMed: 38104859
DOI: 10.1016/j.jmb.2023.168405

実験手法

X-RAY DIFFRACTION (1.5 Å)