1MFT

Crystal Structure Of Four-Helix Bundle Model

1MFT の概要

• エントリーDOI: 10.2210/pdb1mft/pdb
• 関連するPDBエントリー: 1EC5 1JMB 1JMO
• 分子名称: Four-helix bundle model, ZINC ION (3 entities in total)
• 機能のキーワード: alpha-helical bundle, protein design, helix turn helix, de novo protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13085.61

構造登録者

Lahr, S.J.,Stayrook, S.E.,North, B.,Kaplan, J.,Geremia, S.,DeGrado, W. (登録日: 2002-08-13, 公開日: 2004-01-20, 最終更新日: 2024-02-14)

主引用文献

Lahr, S.J.,Engel, D.E.,Stayrook, S.E.,Maglio, O.,North, B.,Geremia, S.,Lombardi, A.,DeGrado, W.F.
Analysis and Design of Turns in alpha-Helical Hairpins
J.Mol.Biol., 346:1441-1454, 2005

PubMed Abstract: Although the analysis and design of turns that connect the strands in antiparallel beta-hairpins has reached an advanced state, much less is known concerning turns between antiparallel helices in helical hairpins. We have conducted an analysis of the structures and sequence preferences of two types of interhelical turns, each of which connects the two helices by a two-residue linker in an alphaL-beta conformation. Based on this analysis, it became apparent that the turn introduced into a designed four-helix bundle protein, DF1, did not occur within an optimal structural context. DF1 is a dimeric model for the diiron class of proteins. A longer loop with a beta-alphaR-beta conformation was inserted between two helices in the protein, and a sequence was chosen to stabilize its conformation. X-ray crystallography and NMR analysis of the protein showed the structure to be in excellent agreement with design.

PubMed: 15713492
DOI: 10.1016/j.jmb.2004.12.016

実験手法

X-RAY DIFFRACTION (2.5 Å)