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The 2.0-�� Crystal Structure of eqFP611, a Far Red Fluorescent Protein from the Sea Anemone Entacmaea quadricolor

Journal Article


Abstract


  • We have crystallized and subsequently determined to 2.0-�� 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 ��-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 ��-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.

Publication Date


  • 2003

Citation


  • Petersen, J., Wilmann, P. G., Beddoe, T., Oakley, A. J., Devenish, R. J., Prescott, M., & Rossjohn, J. (2003). The 2.0-�� Crystal Structure of eqFP611, a Far Red Fluorescent Protein from the Sea Anemone Entacmaea quadricolor. Journal of Biological Chemistry, 278(45), 44626-44631. doi:10.1074/jbc.M307896200

Scopus Eid


  • 2-s2.0-0242666241

Start Page


  • 44626

End Page


  • 44631

Volume


  • 278

Issue


  • 45

Place Of Publication


Abstract


  • We have crystallized and subsequently determined to 2.0-�� 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 ��-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 ��-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.

Publication Date


  • 2003

Citation


  • Petersen, J., Wilmann, P. G., Beddoe, T., Oakley, A. J., Devenish, R. J., Prescott, M., & Rossjohn, J. (2003). The 2.0-�� Crystal Structure of eqFP611, a Far Red Fluorescent Protein from the Sea Anemone Entacmaea quadricolor. Journal of Biological Chemistry, 278(45), 44626-44631. doi:10.1074/jbc.M307896200

Scopus Eid


  • 2-s2.0-0242666241

Start Page


  • 44626

End Page


  • 44631

Volume


  • 278

Issue


  • 45

Place Of Publication