1K50

A V49A Mutation Induces 3D Domain Swapping in the B1 Domain of Protein L from Peptostreptococcus magnus

1K50 の概要

• エントリーDOI: 10.2210/pdb1k50/pdb
• 関連するPDBエントリー: 1HZ5 1HZ6 1JML 1K51 1K52 1K53
• 分子名称: Protein L (2 entities in total)
• 機能のキーワード: protein l b1 domain, strained beta-hairpin turn, positive phi angles, domain swapping, amyloid formation, protein binding
• 由来する生物種: Finegoldia magna
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 27450.01

構造登録者

O'Neill, J.W.,Kim, D.E.,Johnsen, K.,Baker, D.,Zhang, K.Y.J. (登録日: 2001-10-09, 公開日: 2001-12-05, 最終更新日: 2023-08-16)

主引用文献

O'Neill, J.W.,Kim, D.E.,Johnsen, K.,Baker, D.,Zhang, K.Y.
Single-site mutations induce 3D domain swapping in the B1 domain of protein L from Peptostreptococcus magnus.
Structure, 9:1017-1027, 2001

PubMed Abstract: Thermodynamic and kinetic studies of the Protein L B1 domain (Ppl) suggest a folding pathway in which, during the folding transition, the first beta hairpin is formed while the second beta hairpin and the alpha helix are largely unstructured. The same mutations in the two beta turns have opposite effects on the folding and unfolding rates. Three of the four residues composing the second beta turn in Ppl have consecutive positive phi angles, indicating strain in the second beta turn.

PubMed: 11709166
DOI: 10.1016/S0969-2126(01)00667-0

実験手法

X-RAY DIFFRACTION (1.8 Å)