1yzw
From Proteopedia
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|PDB= 1yzw |SIZE=350|CAPTION= <scene name='initialview01'>1yzw</scene>, resolution 2.10Å | |PDB= 1yzw |SIZE=350|CAPTION= <scene name='initialview01'>1yzw</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> | + | |LIGAND= <scene name='pdbligand=CRU:4-[(4Z)-1-(CARBOXYMETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-2-YL]-4-IMINOBUTANOIC+ACID'>CRU</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yzw OCA], [http://www.ebi.ac.uk/pdbsum/1yzw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yzw RCSB]</span> | ||
}} | }} | ||
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[[Category: Rossjohn, J.]] | [[Category: Rossjohn, J.]] | ||
[[Category: Wilmann, P G.]] | [[Category: Wilmann, P G.]] | ||
| - | [[Category: PEG]] | ||
[[Category: luminescent protein]] | [[Category: luminescent protein]] | ||
| - | ''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 01:27:00 2008'' |
Revision as of 22:27, 30 March 2008
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| , resolution 2.10Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The 2.1A Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore
Overview
We have determined the crystal structure of HcRed, a far-red fluorescent protein isolated from Heteractis crispa, to 2.1A resolution. HcRed was observed to form a dimer, in contrast to the monomeric form of green fluorescent protein (GFP) or the tetrameric forms of the GFP-like proteins (eqFP611, Rtms5 and DsRed). Unlike the well-defined chromophore conformation observed in GFP and the GFP-like proteins, the HcRed chromophore was observed to be considerably mobile. Within the HcRed structure, the cyclic tripeptide chromophore, Glu(64)-Tyr(65)-Gly(66), was observed to adopt both a cis coplanar and a trans non-coplanar conformation. As a result of these two conformations, the hydroxyphenyl moiety of the chromophore makes distinct interactions within the interior of the beta-can. These data together with a quantum chemical model of the chromophore, suggest the cis coplanar conformation to be consistent with the fluorescent properties of HcRed, and the trans non-coplanar conformation to be consistent with non-fluorescent properties of hcCP, the chromoprotein parent of HcRed. Moreover, within the GFP-like family, it appears that where conformational freedom is permissible then flexibility in the chromophore conformation is possible.
About this Structure
1YZW is a Single protein structure of sequence from Heteractis crispa. Full crystallographic information is available from OCA.
Reference
The 2.1A crystal structure of the far-red fluorescent protein HcRed: inherent conformational flexibility of the chromophore., Wilmann PG, Petersen J, Pettikiriarachchi A, Buckle AM, Smith SC, Olsen S, Perugini MA, Devenish RJ, Prescott M, Rossjohn J, J Mol Biol. 2005 May 27;349(1):223-37. Epub 2005 Mar 22. PMID:15876379
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