1SN9

An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein

1SN9 の概要

• エントリーDOI: 10.2210/pdb1sn9/pdb
• 関連するPDBエントリー: 1SNA 1SNE
• 分子名称: tetrameric beta-beta-alpha mini-protein (2 entities in total)
• 機能のキーワード: protein design, domain swapping, mini-protein, oligomerization, de novo protein
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 10175.50

構造登録者

Ali, M.H.,Peisach, E.,Allen, K.N.,Imperiali, B. (登録日: 2004-03-10, 公開日: 2004-08-17, 最終更新日: 2024-05-08)

主引用文献

Ali, M.H.,Peisach, E.,Allen, K.N.,Imperiali, B.
X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture
Proc.Natl.Acad.Sci.USA, 101:12183-12188, 2004

PubMed Abstract: The x-ray crystal structure of an oligomeric miniprotein has been determined to a 1.2-A resolution by means of multiwavelength anomalous diffraction phasing with selenomethionine analogs that retain the biophysical characteristics of the native peptide. Peptide 1, comprising alpha and beta secondary structure elements with only 21 aa per monomer, associates as a discrete tetramer. The peptide adopts a previously uncharacterized quaternary structure in which alpha and beta components interact to form a tightly packed and well defined hydrophobic core. The structure provides insight into the origins of the unusual thermal stability of the oligomer. The miniprotein shares many characteristics of larger proteins, including cooperative folding, lack of 1-anilino-8-naphthalene sulfonate binding, and limited deuterium exchange, and possesses a buried surface area typical of native proteins.

PubMed: 15302930
DOI: 10.1073/pnas.0401245101

実験手法

X-RAY DIFFRACTION (1.2 Å)