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zFP538, a yellow-fluorescent protein from Zoanthus, contains a novel three-ring chromophore.
Biochemistry 2005; 44(1):202-12B

Abstract

Crystal structures of the tetrameric yellow-fluorescent protein zFP538 from the button polyp Zoanthus sp. and a green-emitting mutant (K66M) are presented. The atomic models have been refined at 2.7 and 2.5 A resolution, with final crystallographic R factors of 0.206 (R(free) = 0.255) and 0.190 (R(free) = 0.295), respectively, and have excellent stereochemistry. The fold of the protomer is very similar to that of green (GFP) and red (DsRed) fluorescent proteins; however, evidence from crystallography and mass spectrometry suggests that zFP538 contains a three-ring chromophore derived from that of GFP. The yellow-emitting species (lambda(em)(max) = 538 nm) is proposed to result from a transimination reaction in which a transiently appearing DsRed-like acylimine is attacked by the terminal amino group of lysine 66 to form a new six-membered ring, cleaving the polypeptide backbone at the 65-66 position. This extends the chromophore conjugation by an additional double bond compared to GFP, lowering the absorption and emission frequencies. Substitution of lysine 66 with aspartate or glutamate partially converts zFP538 into a red-fluorescent protein, providing additional support for an acylimine intermediate. The diverse and unexpected roles of the side chain at position 66 give new insight into the chemistry of chromophore maturation in the extended family of GFP-like proteins.

Authors+Show Affiliations

Institute of Molecular Biology, Department of Physics, University of Oregon, Eugene, Oregon 97403-1229, USA. jremington@uoxray.uoregon.eduNo 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
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

15628861

Citation

Remington, S James, et al. "ZFP538, a Yellow-fluorescent Protein From Zoanthus, Contains a Novel Three-ring Chromophore." Biochemistry, vol. 44, no. 1, 2005, pp. 202-12.
Remington SJ, Wachter RM, Yarbrough DK, et al. ZFP538, a yellow-fluorescent protein from Zoanthus, contains a novel three-ring chromophore. Biochemistry. 2005;44(1):202-12.
Remington, S. J., Wachter, R. M., Yarbrough, D. K., Branchaud, B., Anderson, D. C., Kallio, K., & Lukyanov, K. A. (2005). ZFP538, a yellow-fluorescent protein from Zoanthus, contains a novel three-ring chromophore. Biochemistry, 44(1), pp. 202-12.
Remington SJ, et al. ZFP538, a Yellow-fluorescent Protein From Zoanthus, Contains a Novel Three-ring Chromophore. Biochemistry. 2005 Jan 11;44(1):202-12. PubMed PMID: 15628861.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - zFP538, a yellow-fluorescent protein from Zoanthus, contains a novel three-ring chromophore. AU - Remington,S James, AU - Wachter,Rebekka M, AU - Yarbrough,Daniel K, AU - Branchaud,Bruce, AU - Anderson,D C, AU - Kallio,Karen, AU - Lukyanov,Konstantin A, PY - 2005/1/5/pubmed PY - 2005/3/5/medline PY - 2005/1/5/entrez SP - 202 EP - 12 JF - Biochemistry JO - Biochemistry VL - 44 IS - 1 N2 - Crystal structures of the tetrameric yellow-fluorescent protein zFP538 from the button polyp Zoanthus sp. and a green-emitting mutant (K66M) are presented. The atomic models have been refined at 2.7 and 2.5 A resolution, with final crystallographic R factors of 0.206 (R(free) = 0.255) and 0.190 (R(free) = 0.295), respectively, and have excellent stereochemistry. The fold of the protomer is very similar to that of green (GFP) and red (DsRed) fluorescent proteins; however, evidence from crystallography and mass spectrometry suggests that zFP538 contains a three-ring chromophore derived from that of GFP. The yellow-emitting species (lambda(em)(max) = 538 nm) is proposed to result from a transimination reaction in which a transiently appearing DsRed-like acylimine is attacked by the terminal amino group of lysine 66 to form a new six-membered ring, cleaving the polypeptide backbone at the 65-66 position. This extends the chromophore conjugation by an additional double bond compared to GFP, lowering the absorption and emission frequencies. Substitution of lysine 66 with aspartate or glutamate partially converts zFP538 into a red-fluorescent protein, providing additional support for an acylimine intermediate. The diverse and unexpected roles of the side chain at position 66 give new insight into the chemistry of chromophore maturation in the extended family of GFP-like proteins. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/15628861/zFP538_a_yellow_fluorescent_protein_from_Zoanthus_contains_a_novel_three_ring_chromophore_ L2 - https://dx.doi.org/10.1021/bi048383r DB - PRIME DP - Unbound Medicine ER -