2b3q: Difference between revisions
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[[Image:2b3q.gif|left|200px]] | [[Image:2b3q.gif|left|200px]] | ||
'''Crystal structure of a well-folded variant of green fluorescent protein''' | {{Structure | ||
|PDB= 2b3q |SIZE=350|CAPTION= <scene name='initialview01'>2b3q</scene>, resolution 2.30Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |||
|ACTIVITY= | |||
|GENE= gft ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 Aequorea victoria]) | |||
}} | |||
'''Crystal structure of a well-folded variant of green fluorescent protein''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2B3Q is a [ | 2B3Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B3Q OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16369541 16369541] | ||
[[Category: Aequorea victoria]] | [[Category: Aequorea victoria]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: 11-stranded beta-barrel]] | [[Category: 11-stranded beta-barrel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:57:11 2008'' | ||
Revision as of 16:57, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Ligands: | |||||||
| Gene: | gft (Aequorea victoria) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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