2g3o: Difference between revisions
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|PDB= 2g3o |SIZE=350|CAPTION= <scene name='initialview01'>2g3o</scene>, resolution 2.100Å | |PDB= 2g3o |SIZE=350|CAPTION= <scene name='initialview01'>2g3o</scene>, resolution 2.100Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=CR2:[2-(METHYLENEAMINE)-4-(4-HYDROXY-BENZYLIDINE)+-5-OXO-4,5-DIHYDRO-IMIDAZOL-1-YL]-ACETALDEHYDE'>CR2</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g3o OCA], [http://www.ebi.ac.uk/pdbsum/2g3o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2g3o RCSB]</span> | |||
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[[Category: gfp]] | [[Category: gfp]] | ||
''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 03:11:26 2008'' | ||
Revision as of 03:11, 31 March 2008
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| , resolution 2.100Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The 2.1A crystal structure of copGFP
OverviewOverview
The green fluorescent protein (avGFP), its variants, and the closely related GFP-like proteins are characterized structurally by a cyclic tri-peptide chromophore located centrally within a conserved beta-can fold. Traditionally, these GFP family members have been isolated from the Cnidaria although recently, distantly related GFP-like proteins from the Bilateria, a sister group of the Cnidaria have been described, although no representative structure from this phylum has been reported to date. We have determined to 2.1A resolution the crystal structure of copGFP, a representative GFP-like protein from a copepod, a member of the Bilateria. The structure of copGFP revealed that, despite sharing only 19% sequence identity with GFP, the tri-peptide chromophore (Gly57-Tyr58-Gly59) of copGFP adopted a cis coplanar conformation within the conserved beta-can fold. However, the immediate environment surrounding the chromophore of copGFP was markedly atypical when compared to other members of the GFP-superfamily, with a large network of bulky residues observed to surround the chromophore. Arg87 and Glu222 (GFP numbering 96 and 222), the only two residues conserved between copGFP, GFP and GFP-like proteins are involved in autocatalytic genesis of the chromophore. Accordingly, the copGFP structure provides an alternative platform for the development of a new suite of fluorescent protein tools. Moreover, the structure suggests that the autocatalytic genesis of the chromophore is remarkably tolerant to a high degree of sequence and structural variation within the beta-can fold of the GFP superfamily.
About this StructureAbout this Structure
2G3O is a Single protein structure of sequence from Pontellina plumata. Full crystallographic information is available from OCA.
ReferenceReference
The 2.1A crystal structure of copGFP, a representative member of the copepod clade within the green fluorescent protein superfamily., Wilmann PG, Battad J, Petersen J, Wilce MC, Dove S, Devenish RJ, Prescott M, Rossjohn J, J Mol Biol. 2006 Jun 16;359(4):890-900. Epub 2006 Apr 25. PMID:16697009
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