2B3P
Crystal structure of a superfolder green fluorescent protein
Summary for 2B3P
| Entry DOI | 10.2210/pdb2b3p/pdb |
| Related | 1EMA 2B3Q |
| Descriptor | green fluorescent protein, CADMIUM ION, ACETIC ACID, ... (4 entities in total) |
| Functional Keywords | 11-stranded beta-barrel, luminescent protein |
| Biological source | Aequorea victoria |
| Total number of polymer chains | 1 |
| Total formula weight | 29144.22 |
| Authors | Pedelacq, J.D.,Cabantous, S.,Tran, T.H.,Terwilliger, T.C.,Waldo, G.S. (deposition date: 2005-09-20, release date: 2005-11-08, Last modification date: 2024-11-13) |
| Primary citation | Pedelacq, J.D.,Cabantous, S.,Tran, T.,Terwilliger, T.C.,Waldo, G.S. Engineering and characterization of a superfolder green fluorescent protein. Nat.Biotechnol., 24:79-88, 2006 Cited by PubMed Abstract: 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. PubMed: 16369541DOI: 10.1038/nbt1172 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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