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Chem Soc Rev. 2009 Oct;38(10):2865-75. doi: 10.1039/b903641p. Epub 2009 Aug 26.

Green fluorescent protein: structure, folding and chromophore maturation.

Author information

1
School of Physics and Astronomy, University of St. Andrews, North Haugh, St. Andrews, UK KY16 9SS. tdc4@st-andrews.ac.uk

Abstract

The prolific use of green fluorescent protein and its variants throughout cellular biology relies on the post-translational formation of the chromophore, which proceeds without the need for any additional enzymes or cofactors, except molecular oxygen. In order to form the mature chromophore, the polypeptide backbone must undergo four distinct processes: folding, cyclisation, oxidation and dehydration. This tutorial review looks in detail at the proposed mechanisms for chromophore formation arising out of experimental and computational studies. The folding process is discussed, and the role that the native state plays in catalysing the initial cyclisation and subsequent chemistry is analysed. The specific functions of four conserved residues (Y66, G67, R96 and E222) in the maturation process are also presented. A greater understanding of the maturation process of fluorescent proteins from both jellyfish and coral species will profit the ongoing quest for brighter, faster maturing, genetically-encodable fluorescent probes of all colours, thus increasing their utility throughout the biomedical sciences.

PMID:
19771333
DOI:
10.1039/b903641p
[Indexed for MEDLINE]

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