1yzw
From Proteopedia
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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 with PEG as ligand. 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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