3AAB

Small heat shock protein hsp14.0 with the mutations of I120F and I122F in the form I crystal

3AAB の概要

• エントリーDOI: 10.2210/pdb3aab/pdb
• 関連するPDBエントリー: 3AAC
• 分子名称: Putative uncharacterized protein ST1653, GLYCEROL, ISOPROPYL ALCOHOL, ... (4 entities in total)
• 機能のキーワード: alpha-crystallin domain, chaperone
• 由来する生物種: Sulfolobus tokodaii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28600.90

構造登録者

Takeda, K.,Hayashi, T.,Abe, T.,Hirano, Y.,Hanazono, Y.,Yohda, M.,Miki, K. (登録日: 2009-11-13, 公開日: 2010-11-17, 最終更新日: 2024-03-13)

主引用文献

Takeda, K.,Hayashi, T.,Abe, T.,Hirano, Y.,Hanazono, Y.,Yohda, M.,Miki, K.
Dimer structure and conformational variability in the N-terminal region of an archaeal small heat shock protein, StHsp14.0
J.Struct.Biol., 174:92-99, 2011

PubMed Abstract: Small heat shock proteins (sHsps), which are categorized into a class of molecular chaperones, bind and stabilize denatured proteins to prevent aggregation. The sHsps undergo transition between different oligomeric states to control their hydrophobicity. So far, only the structures of sHsps in large oligomeric states have been reported. Here we report the structure of StHsp14.0 from Sulfolobus tokodaii in the dimeric state, which is formed by means of a mutation at the C-terminal IXI/V motif. The dimer is the sole building block in two crystal forms, and the dimeric mode is the same as that in the large oligomers. The N-terminal helix has variety in its conformation. Furthermore, spectroscopic and biochemical experiments were performed to investigate the conformational variability at the N-terminus. The structural, dynamical and oligomeric properties suggest that chaperone activity of StHsp14.0 is mediated by partially dissolved oligomers.

PubMed: 21195185
DOI: 10.1016/j.jsb.2010.12.006

実験手法

X-RAY DIFFRACTION (1.851 Å)