The 2.1 Å Crystal Structure of copGFP, a Representative Member of the Copepod Clade Within the Green Fluorescent Protein Superfamily
The green fluorescent protein (avGFP), its variants, and the closely related GFP-like proteins are characterized structurally by a cyclic tri-peptide chromophore located centrally within a conserved β-can fold. Traditionally, these GFP family members have been isolated from the Cnidaria although rec...
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Published in | Journal of molecular biology Vol. 359; no. 4; pp. 890 - 900 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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Elsevier Ltd
01.06.2006
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Abstract | The green fluorescent protein (avGFP), its variants, and the closely related GFP-like proteins are characterized structurally by a cyclic tri-peptide chromophore located centrally within a conserved β-can fold. Traditionally, these GFP family members have been isolated from the Cnidaria although recently, distantly related GFP-like proteins from the Bilateria, a sister group of the Cnidaria have been described, although no representative structure from this phylum has been reported to date. We have determined to 2.1
Å resolution the crystal structure of copGFP, a representative GFP-like protein from a copepod, a member of the Bilateria. The structure of copGFP revealed that, despite sharing only 19% sequence identity with GFP, the tri-peptide chromophore (Gly57-Tyr58-Gly59) of copGFP adopted a
cis coplanar conformation within the conserved β-can fold. However, the immediate environment surrounding the chromophore of copGFP was markedly atypical when compared to other members of the GFP-superfamily, with a large network of bulky residues observed to surround the chromophore. Arg87 and Glu222 (GFP numbering 96 and 222), the only two residues conserved between copGFP, GFP and GFP-like proteins are involved in autocatalytic genesis of the chromophore. Accordingly, the copGFP structure provides an alternative platform for the development of a new suite of fluorescent protein tools. Moreover, the structure suggests that the autocatalytic genesis of the chromophore is remarkably tolerant to a high degree of sequence and structural variation within the β-can fold of the GFP superfamily. |
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AbstractList | The green fluorescent protein (avGFP), its variants, and the closely related GFP-like proteins are characterized structurally by a cyclic tri-peptide chromophore located centrally within a conserved β-can fold. Traditionally, these GFP family members have been isolated from the Cnidaria although recently, distantly related GFP-like proteins from the Bilateria, a sister group of the Cnidaria have been described, although no representative structure from this phylum has been reported to date. We have determined to 2.1
Å resolution the crystal structure of copGFP, a representative GFP-like protein from a copepod, a member of the Bilateria. The structure of copGFP revealed that, despite sharing only 19% sequence identity with GFP, the tri-peptide chromophore (Gly57-Tyr58-Gly59) of copGFP adopted a
cis coplanar conformation within the conserved β-can fold. However, the immediate environment surrounding the chromophore of copGFP was markedly atypical when compared to other members of the GFP-superfamily, with a large network of bulky residues observed to surround the chromophore. Arg87 and Glu222 (GFP numbering 96 and 222), the only two residues conserved between copGFP, GFP and GFP-like proteins are involved in autocatalytic genesis of the chromophore. Accordingly, the copGFP structure provides an alternative platform for the development of a new suite of fluorescent protein tools. Moreover, the structure suggests that the autocatalytic genesis of the chromophore is remarkably tolerant to a high degree of sequence and structural variation within the β-can fold of the GFP superfamily. |
Author | Devenish, Rodney J. Rossjohn, Jamie Prescott, Mark Petersen, Jan Wilce, Matthew C.J. Wilmann, Pascal G. Battad, Jion Dove, Sophie |
Author_xml | – sequence: 1 givenname: Pascal G. surname: Wilmann fullname: Wilmann, Pascal G. organization: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University, Clayton Campus, Vic. 3800, Australia – sequence: 2 givenname: Jion surname: Battad fullname: Battad, Jion organization: Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton Campus, Vic. 3800, Australia – sequence: 3 givenname: Jan surname: Petersen fullname: Petersen, Jan organization: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University, Clayton Campus, Vic. 3800, Australia – sequence: 4 givenname: Matthew C.J. surname: Wilce fullname: Wilce, Matthew C.J. organization: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University, Clayton Campus, Vic. 3800, Australia – sequence: 5 givenname: Sophie surname: Dove fullname: Dove, Sophie organization: Centre for Marine Studies, ARC Centre of Excellence for Coral Reef Studies, University of Queensland, St. Lucia, Qld. 4072, Australia – sequence: 6 givenname: Rodney J. surname: Devenish fullname: Devenish, Rodney J. organization: Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton Campus, Vic. 3800, Australia – sequence: 7 givenname: Mark surname: Prescott fullname: Prescott, Mark email: mark.prescott@med.monash.edu.au organization: Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton Campus, Vic. 3800, Australia – sequence: 8 givenname: Jamie surname: Rossjohn fullname: Rossjohn, Jamie email: jamie.rossjohn@med.monash.edu.au organization: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University, Clayton Campus, Vic. 3800, Australia |
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Keywords | copepoda protein CPs FPs QY vdw GFP structure GFP protein fluorescence ppluGFP2 BSA copGFP r.m.s.d FRET |
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SubjectTerms | copepoda protein copGFP GFP structure protein fluorescence |
Title | The 2.1 Å Crystal Structure of copGFP, a Representative Member of the Copepod Clade Within the Green Fluorescent Protein Superfamily |
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