2b3p

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|PDB= 2b3p |SIZE=350|CAPTION= <scene name='initialview01'>2b3p</scene>, resolution 1.40&Aring;
|PDB= 2b3p |SIZE=350|CAPTION= <scene name='initialview01'>2b3p</scene>, resolution 1.40&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CRO:[2-(1-AMINO-2-HYDROXY-PROPYL)-4-(4-HYDROXY-BENZYLIDINE)-5-OXO-4,5-DIHYDRO-IMIDAZOL-1-YL]-ACETALDEHYDE'>CRO</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= gft ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 Aequorea victoria])
|GENE= gft ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 Aequorea victoria])
 +
|DOMAIN=
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|RELATEDENTRY=[[1ema|1EMA]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b3p OCA], [http://www.ebi.ac.uk/pdbsum/2b3p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b3p RCSB]</span>
}}
}}
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[[Category: Tran, T H.]]
[[Category: Tran, T H.]]
[[Category: Waldo, G S.]]
[[Category: Waldo, G S.]]
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[[Category: ACY]]
 
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[[Category: CD]]
 
[[Category: 11-stranded beta-barrel]]
[[Category: 11-stranded beta-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:57:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:01:02 2008''

Revision as of 23:01, 30 March 2008


PDB ID 2b3p

Drag the structure with the mouse to rotate
, resolution 1.40Å
Ligands: , ,
Gene: gft (Aequorea victoria)
Related: 1EMA


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of a superfolder green fluorescent protein


Overview

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 Structure

2B3P is a Single protein structure of sequence from Aequorea victoria. Full crystallographic information is available from OCA.

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:16369541

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