Mutation L232H Promotes Chromophore Maturation of EGFP-Based Fluorescent Fusion Proteins


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Resumo

The L232H mutant of the enhanced green fluorescent protein (EGFP) was expressed and crystallized. An X-ray diffraction data set was collected from the crystals to 1.53 Å resolution. An analysis of the three-dimensional structure revealed a stacking interaction between the amino-acid residues Н78 and Н232, which contributes to the fastening of the C-terminal region of the protein in the vicinity of the chromophore and influences chromophore maturation of hybrid fluorescent proteins produced by fusion of the target proteins with the C-terminus of EGFP. This hypothesis was experimentally confirmed by investigating chromophore maturation of the hybrid proteins fused to the N- and C-termini of EGFP and EGFP-L232H.

Sobre autores

A. Simanovskaya

National Research Centre “Kurchatov Institute,”

Email: taniarakitina@yahoo.com
Rússia, Moscow, 123098

T. Ivashina

Skryabin Institute of Biochemistry and Physiology of Microorganisms

Email: taniarakitina@yahoo.com
Rússia, Pushchino, Moscow Region, 142290

Y. Zeifman

National Research Centre “Kurchatov Institute,”

Email: taniarakitina@yahoo.com
Rússia, Moscow, 123098

T. Fateeva

National Research Centre “Kurchatov Institute,”

Email: taniarakitina@yahoo.com
Rússia, Moscow, 123098

M. Krukova

National Research Centre “Kurchatov Institute,”

Email: taniarakitina@yahoo.com
Rússia, Moscow, 123098

A. Popov

European Synchrotron Radiation Facility

Email: taniarakitina@yahoo.com
França, Grenoble, 38000

G. Kachalova

National Research Centre “Kurchatov Institute,”; Federal Research Centre “Fundamentals of Biotechnology,”

Email: taniarakitina@yahoo.com
Rússia, Moscow, 123098; Moscow, 119071

T. Rakitina

National Research Centre “Kurchatov Institute,”; Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry

Autor responsável pela correspondência
Email: taniarakitina@yahoo.com
Rússia, Moscow, 123098; Moscow, 117997

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