1YZW
The 2.1A Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore
Summary for 1YZW
| Entry DOI | 10.2210/pdb1yzw/pdb |
| Descriptor | GFP-like non-fluorescent chromoprotein, DI(HYDROXYETHYL)ETHER (3 entities in total) |
| Functional Keywords | luminescent protein |
| Biological source | Heteractis crispa (leathery sea anemone) |
| Total number of polymer chains | 4 |
| Total formula weight | 102812.93 |
| Authors | Wilmann, P.G.,Petersen, J.,Pettikiriarachchi, A.,Buckle, A.M.,Devenish, R.J.,Prescott, M.,Rossjohn, J. (deposition date: 2005-02-28, release date: 2005-05-17, Last modification date: 2024-10-30) |
| Primary citation | Wilmann, P.G.,Petersen, J.,Pettikiriarachchi, A.,Buckle, A.M.,Smith, S.C.,Olsen, S.,Perugini, M.A.,Devenish, R.J.,Prescott, M.,Rossjohn, J. The 2.1A Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore J.Mol.Biol., 349:223-237, 2005 Cited by PubMed Abstract: 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. PubMed: 15876379DOI: 10.1016/j.jmb.2005.03.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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