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The 2.0-A crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor.
J Biol Chem 2003; 278(45):44626-31JB

Abstract

We have crystallized and subsequently determined to 2.0-A resolution the crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor. The structure of the protomer, which adopts a beta-can topology, is similar to that of the related monomeric green fluorescent protein (GFP). The quaternary structure of eqFP611, a tetramer exhibiting 222 symmetry, is similar to that observed for the more closely related red fluorescent protein DsRed and the chromoprotein Rtms5. The unique chromophore sequence (Met63-Tyr64-Gly65) of eqFP611, adopts a coplanar and trans conformation within the interior of the beta-can fold. Accordingly, the eqFP611 chromophore adopts a significantly different conformation in comparison to the chromophore conformation observed in GFP, DsRed, and Rtms5. The coplanar chromophore conformation and its immediate environment provide a structural basis for the far red, highly fluorescent nature of eqFP611. The eqFP611 structure extends our knowledge on the range of conformations a chromophore can adopt within closely related members of the green fluorescent protein family.

Authors+Show Affiliations

The Protein Crystallography Unit, School of Biomedical Sciences, Monash University, Victoria, Australia.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

12909624

Citation

Petersen, Jan, et al. "The 2.0-A Crystal Structure of eqFP611, a Far Red Fluorescent Protein From the Sea Anemone Entacmaea Quadricolor." The Journal of Biological Chemistry, vol. 278, no. 45, 2003, pp. 44626-31.
Petersen J, Wilmann PG, Beddoe T, et al. The 2.0-A crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor. J Biol Chem. 2003;278(45):44626-31.
Petersen, J., Wilmann, P. G., Beddoe, T., Oakley, A. J., Devenish, R. J., Prescott, M., & Rossjohn, J. (2003). The 2.0-A crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor. The Journal of Biological Chemistry, 278(45), pp. 44626-31.
Petersen J, et al. The 2.0-A Crystal Structure of eqFP611, a Far Red Fluorescent Protein From the Sea Anemone Entacmaea Quadricolor. J Biol Chem. 2003 Nov 7;278(45):44626-31. PubMed PMID: 12909624.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The 2.0-A crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor. AU - Petersen,Jan, AU - Wilmann,Pascal G, AU - Beddoe,Travis, AU - Oakley,Aaron J, AU - Devenish,Rodney J, AU - Prescott,Mark, AU - Rossjohn,Jamie, Y1 - 2003/08/08/ PY - 2003/8/12/pubmed PY - 2004/1/6/medline PY - 2003/8/12/entrez SP - 44626 EP - 31 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 278 IS - 45 N2 - We have crystallized and subsequently determined to 2.0-A resolution the crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor. The structure of the protomer, which adopts a beta-can topology, is similar to that of the related monomeric green fluorescent protein (GFP). The quaternary structure of eqFP611, a tetramer exhibiting 222 symmetry, is similar to that observed for the more closely related red fluorescent protein DsRed and the chromoprotein Rtms5. The unique chromophore sequence (Met63-Tyr64-Gly65) of eqFP611, adopts a coplanar and trans conformation within the interior of the beta-can fold. Accordingly, the eqFP611 chromophore adopts a significantly different conformation in comparison to the chromophore conformation observed in GFP, DsRed, and Rtms5. The coplanar chromophore conformation and its immediate environment provide a structural basis for the far red, highly fluorescent nature of eqFP611. The eqFP611 structure extends our knowledge on the range of conformations a chromophore can adopt within closely related members of the green fluorescent protein family. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/12909624/The_2_0_A_crystal_structure_of_eqFP611_a_far_red_fluorescent_protein_from_the_sea_anemone_Entacmaea_quadricolor_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=12909624 DB - PRIME DP - Unbound Medicine ER -