2b3q
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Crystal structure of a well-folded variant of green fluorescent protein
OverviewOverview
Existing variants of green fluorescent protein (GFP) often misfold when, expressed as fusions with other proteins. We have generated a robustly, folded version of GFP, called 'superfolder' GFP, that folds well even when, fused to poorly folded polypeptides. Compared to 'folding reporter' GFP, a, folding-enhanced GFP containing the 'cycle-3' mutations and the 'enhanced, GFP' mutations F64L and S65T, superfolder GFP shows improved tolerance of, circular permutation, greater resistance to chemical denaturants and, improved folding kinetics. The fluorescence of Escherichia coli cells, expressing each of eighteen proteins from Pyrobaculum aerophilum as, fusions with superfolder GFP was proportional to total protein expression., In contrast, fluorescence of folding reporter GFP fusion proteins was, strongly correlated with the productive folding yield of the passenger, protein. X-ray crystallographic structural analyses helped explain the, enhanced folding of superfolder GFP relative to folding reporter GFP.
About this StructureAbout this Structure
2B3Q is a Single protein structure of sequence from Aequorea victoria with MG as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Engineering and characterization of a superfolder green fluorescent protein., Pedelacq JD, Cabantous S, Tran T, Terwilliger TC, Waldo GS, Nat Biotechnol. 2006 Jan;24(1):79-88. Epub 2005 Dec 20. PMID:16369541
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