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5LTQ

Structure of the Yellow Fluorescent Protein lanYFP from Branchiostoma lanceolatum at pH 7.5

Summary for 5LTQ
Entry DOI10.2210/pdb5ltq/pdb
DescriptorGreen fluorescent protein blFP-Y3, CHLORIDE ION (3 entities in total)
Functional Keywordsfluorescent protein
Biological sourceBranchiostoma lanceolatum (Common lancelet)
Total number of polymer chains16
Total formula weight485846.43
Authors
Clavel, D.,Gotthard, G.,Royant, A. (deposition date: 2016-09-07, release date: 2016-12-07, Last modification date: 2024-01-17)
Primary citationClavel, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

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건을2024-11-06부터공개중

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