1KH0

Accurate Computer Base Design of a New Backbone Conformation in the Second Turn of Protein L

1KH0 の概要

• エントリーDOI: 10.2210/pdb1kh0/pdb
• 関連するPDBエントリー: 1HZ5 1HZ6
• 分子名称: protein L (2 entities in total)
• 機能のキーワード: protein l b1 domain, computational based protein design, type 1' beta turn, extensive amino acid mutations., protein binding
• 由来する生物種: Finegoldia magna
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 14248.17

構造登録者

O'Neill, J.W.,Kuhlman, B.,Kim, D.E.,Zhang, K.Y.,Baker, D. (登録日: 2001-11-28, 公開日: 2002-01-23, 最終更新日: 2023-08-16)

主引用文献

Kuhlman, B.,O'Neill, J.W.,Kim, D.E.,Zhang, K.Y.,Baker, D.
Accurate computer-based design of a new backbone conformation in the second turn of protein L.
J.Mol.Biol., 315:471-477, 2002

PubMed Abstract: The rational design of loops and turns is a key step towards creating proteins with new functions. We used a computational design procedure to create new backbone conformations in the second turn of protein L. The Protein Data Bank was searched for alternative turn conformations, and sequences optimal for these turns in the context of protein L were identified using a Monte Carlo search procedure and an energy function that favors close packing. Two variants containing 12 and 14 mutations were found to be as stable as wild-type protein L. The crystal structure of one of the variants has been solved at a resolution of 1.9 A, and the backbone conformation in the second turn is remarkably close to that of the in silico model (1.1 A RMSD) while it differs significantly from that of wild-type protein L (the turn residues are displaced by an average of 7.2 A). The folding rates of the redesigned proteins are greater than that of the wild-type protein and in contrast to wild-type protein L the second beta-turn appears to be formed at the rate limiting step in folding.

PubMed: 11786026
DOI: 10.1006/jmbi.2001.5229

実験手法

X-RAY DIFFRACTION (1.9 Å)