3AI5

Crystal structure of yeast enhanced green fluorescent protein-ubiquitin fusion protein

3AI5 の概要

• エントリーDOI: 10.2210/pdb3ai5/pdb
• 関連するPDBエントリー: 3AI4
• 分子名称: yeast enhanced green fluorescent protein,Ubiquitin, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: green fluorescent protein, ubiquitin, fusion protein, fluorescent protein, transcription
• 由来する生物種: Aequorea victoria (Jellyfish); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35061.60

構造登録者

Suzuki, N.,Wakatsuki, S.,Kawasaki, M. (登録日: 2010-05-10, 公開日: 2010-09-29, 最終更新日: 2024-11-20)

主引用文献

Suzuki, N.,Hiraki, M.,Yamada, Y.,Matsugaki, N.,Igarashi, N.,Kato, R.,Dikic, I.,Drew, D.,Iwata, S.,Wakatsuki, S.,Kawasaki, M.
Crystallization of small proteins assisted by green fluorescent protein
Acta Crystallogr.,Sect.D, 66:1059-1066, 2010

PubMed Abstract: The generation of crystal lattice contacts by proteinaceous tags fused to target proteins is an attractive approach to aid in the crystallization of otherwise intractable proteins. Here, the use of green fluorescent protein (GFP) fusions for this purpose is demonstrated, using ubiquitin and the ubiquitin-binding motif (UBM) of Y-family polymerase ι as examples. The structure of the GFP-ubiquitin fusion protein revealed that the crystal lattice was formed by GFP moieties. Ubiquitin was accommodated in the lattice through interactions with the peripheral loops of GFP. However, in the GFP-UBM fusion crystal UBM formed extensive interactions with GFP and these interactions, together with UBM dimerization, mediated the crystal packing. Interestingly, the tyrosine residues that are involved in mediating crystal contacts in both GFP-ubiquitin and GFP-UBM crystals are arranged in a belt on the surface of the β-barrel structure of GFP. Therefore, it is likely that GFP can assist in the crystallization of small proteins and of protein domains in general.

PubMed: 20944239
DOI: 10.1107/S0907444910032944

実験手法

X-RAY DIFFRACTION (1.4 Å)