Structural Factors Enabling Successful GFP-Like Proteins with Alanine as the Third Chromophore-Forming Residue

Autor:	Liya Muslinkina, Abigail Roldán-Salgado, Paul Gaytán, Víctor R. Juárez-González, Enrique Rudiño, Nadya Pletneva, Vladimir Pletnev, Zbigniew Dauter, Sergei Pletnev
Rok vydání:	2019
Předmět:	Models Molecular Alanine Protein Conformation Green Fluorescent Proteins Glycine Crystallography X-Ray Article Mutagenesis Sequence Analysis Protein Structural Biology Mutation Animals Amino Acid Sequence Molecular Biology Lancelets
Zdroj:	Journal of Molecular Biology. 431:1397-1408
ISSN:	0022-2836
DOI:	10.1016/j.jmb.2019.02.013
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4da4f413aa3eb494eafd99c911d7cc9c https://doi.org/10.1016/j.jmb.2019.02.013 Zobrazit plný text záznamu Full Text from ScienceDirect