Tags

Type your tag names separated by a space and hit enter

Crystallographic study of red fluorescent protein eqFP578 and its far-red variant Katushka reveals opposite pH-induced isomerization of chromophore.
Protein Sci 2011; 20(7):1265-74PS

Abstract

The wild type red fluorescent protein eqFP578 (from sea anemone Entacmaea quadricolor, λ(ex) = 552 nm, λ(em) = 578 nm) and its bright far-red fluorescent variant Katushka (λ(ex) = 588 nm, λ(em) = 635 nm) are characterized by the pronounced pH dependence of their fluorescence. The crystal structures of eqFP578f (eqFP578 with two point mutations improving the protein folding) and Katushka have been determined at the resolution ranging from 1.15 to 1.85 Å at two pH values, corresponding to low and high level of fluorescence. The observed extinguishing of fluorescence upon reducing pH in eqFP578f and Katushka has been shown to be accompanied by the opposite trans-cis and cis-trans chromophore isomerization, respectively. Asn143, Ser158, His197 and Ser143, Leu174, and Arg197 have been shown to stabilize the respective trans and cis fluorescent states of the chromophores in eqFP578f and Katushka at higher pH. The cis state has been suggested as being primarily responsible for the observed far-red shift of the emission maximum of Katushka relative to that of eqFP578f.

Authors+Show Affiliations

Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Science, Moscow 117997, Miklukho-Maklaya 16/10, Russia. pletnevs@mail.nih.govNo 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, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

21563226

Citation

Pletneva, Nadya V., et al. "Crystallographic Study of Red Fluorescent Protein eqFP578 and Its Far-red Variant Katushka Reveals Opposite pH-induced Isomerization of Chromophore." Protein Science : a Publication of the Protein Society, vol. 20, no. 7, 2011, pp. 1265-74.
Pletneva NV, Pletnev VZ, Shemiakina II, et al. Crystallographic study of red fluorescent protein eqFP578 and its far-red variant Katushka reveals opposite pH-induced isomerization of chromophore. Protein Sci. 2011;20(7):1265-74.
Pletneva, N. V., Pletnev, V. Z., Shemiakina, I. I., Chudakov, D. M., Artemyev, I., Wlodawer, A., ... Pletnev, S. (2011). Crystallographic study of red fluorescent protein eqFP578 and its far-red variant Katushka reveals opposite pH-induced isomerization of chromophore. Protein Science : a Publication of the Protein Society, 20(7), pp. 1265-74. doi:10.1002/pro.654.
Pletneva NV, et al. Crystallographic Study of Red Fluorescent Protein eqFP578 and Its Far-red Variant Katushka Reveals Opposite pH-induced Isomerization of Chromophore. Protein Sci. 2011;20(7):1265-74. PubMed PMID: 21563226.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallographic study of red fluorescent protein eqFP578 and its far-red variant Katushka reveals opposite pH-induced isomerization of chromophore. AU - Pletneva,Nadya V, AU - Pletnev,Vladimir Z, AU - Shemiakina,Irina I, AU - Chudakov,Dmitriy M, AU - Artemyev,Igor, AU - Wlodawer,Alexander, AU - Dauter,Zbigniew, AU - Pletnev,Sergei, Y1 - 2011/06/10/ PY - 2011/02/28/received PY - 2011/04/25/revised PY - 2011/04/26/accepted PY - 2011/5/13/entrez PY - 2011/5/13/pubmed PY - 2011/10/25/medline SP - 1265 EP - 74 JF - Protein science : a publication of the Protein Society JO - Protein Sci. VL - 20 IS - 7 N2 - The wild type red fluorescent protein eqFP578 (from sea anemone Entacmaea quadricolor, λ(ex) = 552 nm, λ(em) = 578 nm) and its bright far-red fluorescent variant Katushka (λ(ex) = 588 nm, λ(em) = 635 nm) are characterized by the pronounced pH dependence of their fluorescence. The crystal structures of eqFP578f (eqFP578 with two point mutations improving the protein folding) and Katushka have been determined at the resolution ranging from 1.15 to 1.85 Å at two pH values, corresponding to low and high level of fluorescence. The observed extinguishing of fluorescence upon reducing pH in eqFP578f and Katushka has been shown to be accompanied by the opposite trans-cis and cis-trans chromophore isomerization, respectively. Asn143, Ser158, His197 and Ser143, Leu174, and Arg197 have been shown to stabilize the respective trans and cis fluorescent states of the chromophores in eqFP578f and Katushka at higher pH. The cis state has been suggested as being primarily responsible for the observed far-red shift of the emission maximum of Katushka relative to that of eqFP578f. SN - 1469-896X UR - https://www.unboundmedicine.com/medline/citation/21563226/Crystallographic_study_of_red_fluorescent_protein_eqFP578_and_its_far_red_variant_Katushka_reveals_opposite_pH_induced_isomerization_of_chromophore_ L2 - https://doi.org/10.1002/pro.654 DB - PRIME DP - Unbound Medicine ER -