Structural and biochemical characterization of the bilin lyase cpcs from thermosynechococcus elongatus

Christina M. Kronfel; Alexandre P. Kuzin; Farhad Forouhar; Avijit Biswas; Min Su; Scott Lew; Jayaraman Seetharaman; Rong Xiao; John K. Everett; Li Chung Ma; Thomas B. Acton; Gaetano T. Montelione; John F. Hunt; Corry E.C. Paul; Tierna M. Dragomani; M. Nazim Boutaghou; Richard B. Cole; Christian Riml; Richard M. Alvey; Donald A. Bryant; Wendy M. Schluchter

doi:10.1021/bi401192z

Structural and biochemical characterization of the bilin lyase cpcs from thermosynechococcus elongatus

Christina M. Kronfel, Alexandre P. Kuzin, Farhad Forouhar, Avijit Biswas, Min Su, Scott Lew, Jayaraman Seetharaman, Rong Xiao, John K. Everett, Li Chung Ma, Thomas B. Acton, Gaetano T. Montelione, John F. Hunt, Corry E.C. Paul, Tierna M. Dragomani, M. Nazim Boutaghou, Richard B. Cole, Christian Riml, Richard M. Alvey, Donald A. BryantWendy M. Schluchter

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

25 Scopus citations

Abstract

Cyanobacterial phycobiliproteins have evolved to capture light energy over most of the visible spectrum due to their bilin chromophores, which are linear tetrapyrroles that have been covalently attached by enzymes called bilin lyases. We report here the crystal structure of a bilin lyase of the CpcS family from Thermosynechococcus elongatus (TeCpcS-III). TeCpcS-III is a 10-stranded β barrel with two alpha helices and belongs to the lipocalin structural family. TeCpcS-III catalyzes both cognate as well as noncognate bilin attachment to a variety of phycobiliprotein subunits. TeCpcS-III ligates phycocyanobilin, phycoerythrobilin, and phytochromobilin to the alpha and beta subunits of allophycocyanin and to the beta subunit of phycocyanin at the Cys82-equivalent position in all cases. The active form of TeCpcS-III is a dimer, which is consistent with the structure observed in the crystal. With the use of the UnaG protein and its association with bilirubin as a guide, a model for the association between the native substrate, phycocyanobilin, and TeCpcS was produced.

Original language	English (US)
Pages (from-to)	8663-8676
Number of pages	14
Journal	Biochemistry
Volume	52
Issue number	48
DOIs	https://doi.org/10.1021/bi401192z
State	Published - Dec 3 2013

All Science Journal Classification (ASJC) codes

Biochemistry

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10.1021/bi401192z

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Kronfel, C. M., Kuzin, A. P., Forouhar, F., Biswas, A., Su, M., Lew, S., Seetharaman, J., Xiao, R., Everett, J. K., Ma, L. C., Acton, T. B., Montelione, G. T., Hunt, J. F., Paul, C. E. C., Dragomani, T. M., Boutaghou, M. N., Cole, R. B., Riml, C., Alvey, R. M., ... Schluchter, W. M. (2013). Structural and biochemical characterization of the bilin lyase cpcs from thermosynechococcus elongatus. Biochemistry, 52(48), 8663-8676. https://doi.org/10.1021/bi401192z

@article{d2abc4841bd54d31baef3e8a90c67716,

title = "Structural and biochemical characterization of the bilin lyase cpcs from thermosynechococcus elongatus",

abstract = "Cyanobacterial phycobiliproteins have evolved to capture light energy over most of the visible spectrum due to their bilin chromophores, which are linear tetrapyrroles that have been covalently attached by enzymes called bilin lyases. We report here the crystal structure of a bilin lyase of the CpcS family from Thermosynechococcus elongatus (TeCpcS-III). TeCpcS-III is a 10-stranded β barrel with two alpha helices and belongs to the lipocalin structural family. TeCpcS-III catalyzes both cognate as well as noncognate bilin attachment to a variety of phycobiliprotein subunits. TeCpcS-III ligates phycocyanobilin, phycoerythrobilin, and phytochromobilin to the alpha and beta subunits of allophycocyanin and to the beta subunit of phycocyanin at the Cys82-equivalent position in all cases. The active form of TeCpcS-III is a dimer, which is consistent with the structure observed in the crystal. With the use of the UnaG protein and its association with bilirubin as a guide, a model for the association between the native substrate, phycocyanobilin, and TeCpcS was produced.",

author = "Kronfel, {Christina M.} and Kuzin, {Alexandre P.} and Farhad Forouhar and Avijit Biswas and Min Su and Scott Lew and Jayaraman Seetharaman and Rong Xiao and Everett, {John K.} and Ma, {Li Chung} and Acton, {Thomas B.} and Montelione, {Gaetano T.} and Hunt, {John F.} and Paul, {Corry E.C.} and Dragomani, {Tierna M.} and Boutaghou, {M. Nazim} and Cole, {Richard B.} and Christian Riml and Alvey, {Richard M.} and Bryant, {Donald A.} and Schluchter, {Wendy M.}",

year = "2013",

month = dec,

day = "3",

doi = "10.1021/bi401192z",

language = "English (US)",

volume = "52",

pages = "8663--8676",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

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Kronfel, CM, Kuzin, AP, Forouhar, F, Biswas, A, Su, M, Lew, S, Seetharaman, J, Xiao, R, Everett, JK, Ma, LC, Acton, TB, Montelione, GT, Hunt, JF, Paul, CEC, Dragomani, TM, Boutaghou, MN, Cole, RB, Riml, C, Alvey, RM, Bryant, DA & Schluchter, WM 2013, 'Structural and biochemical characterization of the bilin lyase cpcs from thermosynechococcus elongatus', Biochemistry, vol. 52, no. 48, pp. 8663-8676. https://doi.org/10.1021/bi401192z

TY - JOUR

T1 - Structural and biochemical characterization of the bilin lyase cpcs from thermosynechococcus elongatus

AU - Kronfel, Christina M.

AU - Kuzin, Alexandre P.

AU - Forouhar, Farhad

AU - Biswas, Avijit

AU - Su, Min

AU - Lew, Scott

AU - Seetharaman, Jayaraman

AU - Xiao, Rong

AU - Everett, John K.

AU - Ma, Li Chung

AU - Acton, Thomas B.

AU - Montelione, Gaetano T.

AU - Hunt, John F.

AU - Paul, Corry E.C.

AU - Dragomani, Tierna M.

AU - Boutaghou, M. Nazim

AU - Cole, Richard B.

AU - Riml, Christian

AU - Alvey, Richard M.

AU - Bryant, Donald A.

AU - Schluchter, Wendy M.

PY - 2013/12/3

Y1 - 2013/12/3

N2 - Cyanobacterial phycobiliproteins have evolved to capture light energy over most of the visible spectrum due to their bilin chromophores, which are linear tetrapyrroles that have been covalently attached by enzymes called bilin lyases. We report here the crystal structure of a bilin lyase of the CpcS family from Thermosynechococcus elongatus (TeCpcS-III). TeCpcS-III is a 10-stranded β barrel with two alpha helices and belongs to the lipocalin structural family. TeCpcS-III catalyzes both cognate as well as noncognate bilin attachment to a variety of phycobiliprotein subunits. TeCpcS-III ligates phycocyanobilin, phycoerythrobilin, and phytochromobilin to the alpha and beta subunits of allophycocyanin and to the beta subunit of phycocyanin at the Cys82-equivalent position in all cases. The active form of TeCpcS-III is a dimer, which is consistent with the structure observed in the crystal. With the use of the UnaG protein and its association with bilirubin as a guide, a model for the association between the native substrate, phycocyanobilin, and TeCpcS was produced.

AB - Cyanobacterial phycobiliproteins have evolved to capture light energy over most of the visible spectrum due to their bilin chromophores, which are linear tetrapyrroles that have been covalently attached by enzymes called bilin lyases. We report here the crystal structure of a bilin lyase of the CpcS family from Thermosynechococcus elongatus (TeCpcS-III). TeCpcS-III is a 10-stranded β barrel with two alpha helices and belongs to the lipocalin structural family. TeCpcS-III catalyzes both cognate as well as noncognate bilin attachment to a variety of phycobiliprotein subunits. TeCpcS-III ligates phycocyanobilin, phycoerythrobilin, and phytochromobilin to the alpha and beta subunits of allophycocyanin and to the beta subunit of phycocyanin at the Cys82-equivalent position in all cases. The active form of TeCpcS-III is a dimer, which is consistent with the structure observed in the crystal. With the use of the UnaG protein and its association with bilirubin as a guide, a model for the association between the native substrate, phycocyanobilin, and TeCpcS was produced.

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UR - http://www.scopus.com/inward/citedby.url?scp=84889247259&partnerID=8YFLogxK

U2 - 10.1021/bi401192z

DO - 10.1021/bi401192z

M3 - Article

C2 - 24215428

AN - SCOPUS:84889247259

SN - 0006-2960

VL - 52

SP - 8663

EP - 8676

JO - Biochemistry

JF - Biochemistry

IS - 48

ER -

Structural and biochemical characterization of the bilin lyase cpcs from thermosynechococcus elongatus

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