1hcj
From Proteopedia
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PHOTOPRODUCT OF THE WILD-TYPE AEQUOREA VICTORIA GREEN FLUORESCENT PROTEIN
Overview
Wild type green fluorescent protein (GFP) from Aequorea victoria absorbs, predominantly at 398 nm. Illumination with UV (254 nm) or visible (390 nm), light transforms this state (GFP(398)) into one absorbing at 483 nm, (GFP(483)). Here we show that this photoconversion of GFP is a one-photon, process that is paralleled by decarboxylation of Glu 222. We propose a, mechanism in which decarboxylation is due to electron transfer between the, gamma-carboxylate of Glu 222 and the p-hydroxybenzylidene-imidazolidinone, chromophore of GFP, followed by reverse transfer of an electron and a, proton to the remaining carbon side chain atom of Glu 222. Oxidative, decarboxylation of a gamma-carboxylate represents a new type of, posttranslational modification that may also occur in enzymes with, high-potential reaction intermediates.
About this Structure
1HCJ is a Single protein structure of sequence from Aequorea victoria. Full crystallographic information is available from OCA.
Reference
Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222., van Thor JJ, Gensch T, Hellingwerf KJ, Johnson LN, Nat Struct Biol. 2002 Jan;9(1):37-41. PMID:11740505
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