6MAS

X-ray Structure of Branchiostoma floridae fluorescent protein lanFP10G

6MAS の概要

• エントリーDOI: 10.2210/pdb6mas/pdb
• 分子名称: Uncharacterized protein, GLYCEROL (3 entities in total)
• 機能のキーワード: gly-tyr-gly chromophore, fluorescent protein
• 由来する生物種: Branchiostoma floridae (Florida lancelet)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 208150.82

構造登録者

Muslinkina, L.,Pletneva, N.,Pletnev, V.,Pletnev, S. (登録日: 2018-08-28, 公開日: 2019-03-13, 最終更新日: 2024-10-23)

主引用文献

Muslinkina, L.,Roldan-Salgado, A.,Gaytan, P.,Juarez-Gonzalez, V.R.,Rudino, E.,Pletneva, N.,Pletnev, V.,Dauter, Z.,Pletnev, S.
Structural Factors Enabling Successful GFP-Like Proteins with Alanine as the Third Chromophore-Forming Residue.
J. Mol. Biol., 431:1397-1408, 2019

PubMed Abstract: GFP-like proteins from lancelets (lanFPs) is a new and least studied group that already generated several outstanding biomarkers (mNeonGreen is the brightest FP to date) and has some unique features. Here, we report the study of four homologous lanFPs with GYG and GYA chromophores. Until recently, it was accepted that the third chromophore-forming residue in GFP-like proteins should be glycine, and efforts to replace it were in vain. Now, we have the first structure of a fluorescent protein with a successfully matured chromophore that has alanine as the third chromophore-forming residue. Consideration of the protein structures revealed two alternative routes of posttranslational transformation, resulting in either chromophore maturation or hydrolysis of GYG/GYA tripeptide. Both transformations are catalyzed by the same set of catalytic residues, Arg88 and Glu35-Wat-Glu211 cluster, whereas the residues in positions 62 and 102 shift the equilibrium between chromophore maturation and hydrolysis.

PubMed: 30797856
DOI: 10.1016/j.jmb.2019.02.013

実験手法

X-RAY DIFFRACTION (1.3 Å)