2g3d
From Proteopedia
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|PDB= 2g3d |SIZE=350|CAPTION= <scene name='initialview01'>2g3d</scene>, resolution 1.35Å | |PDB= 2g3d |SIZE=350|CAPTION= <scene name='initialview01'>2g3d</scene>, resolution 1.35Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= GFP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 Aequorea victoria]) | |GENE= GFP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 Aequorea victoria]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2g16|2G16]], [[2g2s|2G2S]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g3d OCA], [http://www.ebi.ac.uk/pdbsum/2g3d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2g3d RCSB]</span> | ||
}} | }} | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Barondeau, D P.]] | [[Category: Barondeau, D P.]] | ||
| - | [[Category: MG]] | ||
[[Category: biosynthesis]] | [[Category: biosynthesis]] | ||
[[Category: chromophore]] | [[Category: chromophore]] | ||
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[[Category: post-translational modification]] | [[Category: post-translational modification]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:11:19 2008'' |
Revision as of 00:11, 31 March 2008
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| , resolution 1.35Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | GFP (Aequorea victoria) | ||||||
| Related: | 2G16, 2G2S
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of S65G Y66A GFP variant after spontaneous peptide hydrolysis
Overview
The green fluorescent protein (GFP) creates a fluorophore out of three sequential amino acids by promoting spontaneous posttranslational modifications. Here, we use high-resolution crystallography to characterize GFP variants that not only undergo peptide backbone cyclization but additional denaturation-induced peptide backbone fragmentation, native peptide hydrolysis, and decarboxylation reactions. Our analyses indicate that architectural features that favor GFP peptide cyclization also drive peptide hydrolysis. These results are relevant for the maturation pathways of GFP homologues, such as the kindling fluorescent protein and the Kaede protein, which use backbone cleavage to red-shift the spectral properties of their chromophores. We further propose a photochemical mechanism for the decarboxylation reaction, supporting a role for the GFP protein environment in facilitating radical formation and one-electron chemistry, which may be important in activating oxygen for the oxidation step of chromophore biosynthesis. Together, our results characterize GFP posttranslational modification chemistry with implications for the energetic landscape of backbone cyclization and subsequent reactions, and for the rational design of predetermined spontaneous backbone cyclization and cleavage reactions.
About this Structure
2G3D is a Protein complex structure of sequences from Aequorea victoria. Full crystallographic information is available from OCA.
Reference
Understanding GFP posttranslational chemistry: structures of designed variants that achieve backbone fragmentation, hydrolysis, and decarboxylation., Barondeau DP, Kassmann CJ, Tainer JA, Getzoff ED, J Am Chem Soc. 2006 Apr 12;128(14):4685-93. PMID:16594705
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