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The 2.1A crystal structure of the far-red fluorescent protein HcRed: inherent conformational flexibility of the chromophore.
J Mol Biol. 2005 May 27; 349(1):223-37.JM

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.

Authors+Show Affiliations

The Protein Crystallography Unit, Monash Centre for Synchrotron Science, School of Biomedical Sciences, Monash University, Clayton, Vic. 3800, Australia.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15876379

Citation

Wilmann, Pascal G., et al. "The 2.1A Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore." Journal of Molecular Biology, vol. 349, no. 1, 2005, pp. 223-37.
Wilmann PG, Petersen J, Pettikiriarachchi A, et al. The 2.1A crystal structure of the far-red fluorescent protein HcRed: inherent conformational flexibility of the chromophore. J Mol Biol. 2005;349(1):223-37.
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. (2005). The 2.1A crystal structure of the far-red fluorescent protein HcRed: inherent conformational flexibility of the chromophore. Journal of Molecular Biology, 349(1), 223-37.
Wilmann PG, et al. The 2.1A Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore. J Mol Biol. 2005 May 27;349(1):223-37. PubMed PMID: 15876379.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The 2.1A crystal structure of the far-red fluorescent protein HcRed: inherent conformational flexibility of the chromophore. AU - Wilmann,Pascal G, AU - Petersen,Jan, AU - Pettikiriarachchi,Anne, AU - Buckle,Ashley M, AU - Smith,Sean C, AU - Olsen,Seth, AU - Perugini,Matthew A, AU - Devenish,Rodney J, AU - Prescott,Mark, AU - Rossjohn,Jamie, Y1 - 2005/03/22/ PY - 2004/12/22/received PY - 2005/03/01/revised PY - 2005/03/05/accepted PY - 2005/5/7/pubmed PY - 2005/6/23/medline PY - 2005/5/7/entrez SP - 223 EP - 37 JF - Journal of molecular biology JO - J. Mol. Biol. VL - 349 IS - 1 N2 - 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. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/15876379/The_2_1A_crystal_structure_of_the_far_red_fluorescent_protein_HcRed:_inherent_conformational_flexibility_of_the_chromophore_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(05)00288-3 DB - PRIME DP - Unbound Medicine ER -