5LTP

Structure of the Yellow-Green Fluorescent Protein mNeonGreen from Branchiostoma lanceolatum at the acidic pH 4.5

5LTP の概要

• エントリーDOI: 10.2210/pdb5ltp/pdb
• 分子名称: mNeonGreen, CHLORIDE ION, CITRATE ANION, ... (4 entities in total)
• 機能のキーワード: fluorescent protein
• 由来する生物種: Branchiostoma lanceolatum
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 184699.40

構造登録者

Clavel, D.,Gotthard, G.,Royant, A. (登録日: 2016-09-07, 公開日: 2016-12-21, 最終更新日: 2024-10-09)

主引用文献

Clavel, D.,Gotthard, G.,von Stetten, D.,De Sanctis, D.,Pasquier, H.,Lambert, G.G.,Shaner, N.C.,Royant, A.
Structural analysis of the bright monomeric yellow-green fluorescent protein mNeonGreen obtained by directed evolution.
Acta Crystallogr D Struct Biol, 72:1298-1307, 2016

PubMed Abstract: Until recently, genes coding for homologues of the autofluorescent protein GFP had only been identified in marine organisms from the phyla Cnidaria and Arthropoda. New fluorescent-protein genes have now been found in the phylum Chordata, coding for particularly bright oligomeric fluorescent proteins such as the tetrameric yellow fluorescent protein lanYFP from Branchiostoma lanceolatum. A successful monomerization attempt led to the development of the bright yellow-green fluorescent protein mNeonGreen. The structures of lanYFP and mNeonGreen have been determined and compared in order to rationalize the directed evolution process leading from a bright, tetrameric to a still bright, monomeric fluorescent protein. An unusual discolouration of crystals of mNeonGreen was observed after X-ray data collection, which was investigated using a combination of X-ray crystallography and UV-visible absorption and Raman spectroscopies, revealing the effects of specific radiation damage in the chromophore cavity. It is shown that X-rays rapidly lead to the protonation of the phenolate O atom of the chromophore and to the loss of its planarity at the methylene bridge.

PubMed: 27917830
DOI: 10.1107/S2059798316018623

実験手法

X-RAY DIFFRACTION (1.7 Å)