2B3P

Crystal structure of a superfolder green fluorescent protein

2B3P の概要

• エントリーDOI: 10.2210/pdb2b3p/pdb
• 関連するPDBエントリー: 1EMA 2B3Q
• 分子名称: green fluorescent protein, CADMIUM ION, ACETIC ACID, ... (4 entities in total)
• 機能のキーワード: 11-stranded beta-barrel, luminescent protein
• 由来する生物種: Aequorea victoria
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29144.22

構造登録者

Pedelacq, J.D.,Cabantous, S.,Tran, T.H.,Terwilliger, T.C.,Waldo, G.S. (登録日: 2005-09-20, 公開日: 2005-11-08, 最終更新日: 2024-11-13)

主引用文献

Pedelacq, J.D.,Cabantous, S.,Tran, T.,Terwilliger, T.C.,Waldo, G.S.
Engineering and characterization of a superfolder green fluorescent protein.
Nat.Biotechnol., 24:79-88, 2006

PubMed Abstract: Existing variants of green fluorescent protein (GFP) often misfold when expressed as fusions with other proteins. We have generated a robustly folded version of GFP, called 'superfolder' GFP, that folds well even when fused to poorly folded polypeptides. Compared to 'folding reporter' GFP, a folding-enhanced GFP containing the 'cycle-3' mutations and the 'enhanced GFP' mutations F64L and S65T, superfolder GFP shows improved tolerance of circular permutation, greater resistance to chemical denaturants and improved folding kinetics. The fluorescence of Escherichia coli cells expressing each of eighteen proteins from Pyrobaculum aerophilum as fusions with superfolder GFP was proportional to total protein expression. In contrast, fluorescence of folding reporter GFP fusion proteins was strongly correlated with the productive folding yield of the passenger protein. X-ray crystallographic structural analyses helped explain the enhanced folding of superfolder GFP relative to folding reporter GFP.

PubMed: 16369541
DOI: 10.1038/nbt1172

実験手法

X-RAY DIFFRACTION (1.4 Å)