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Title: Structural and spectroscopic characterization of HCP2

Abstract

The Helical Carotenoid Proteins (HCPs) are a large group of newly identified carotenoid-binding proteins found in ecophysiologically diverse cyanobacteria. They likely evolved before becoming the effector (quenching) domain of the modular Orange Carotenoid Protein (OCP). The number of discrete HCP families—at least nine—suggests they are involved in multiple distinct functions. Here we report the 1.7 Å crystal structure of HCP2, one of the most widespread HCPs found in nature, from the chromatically acclimating cyanobacterium Tolypothrix sp. PCC 7601. By purifying HCP2 from the native source we are able to identify its natively-bound carotenoid, which is exclusively canthaxanthin. In solution, HCP2 is a monomer with an absorbance maximum of 530 nm. However, the HCP2 crystals have a maximum absorbance at 548 nm, which is accounted by the stacking of the β1 rings of the carotenoid in the two molecules in the asymmetric unit. Our results demonstrate how HCPs provide a valuable system to study carotenoid-protein interactions and their spectroscopic implications, and contribute to efforts to understand the functional roles of this large, newly discovered family of pigment proteins, which to-date remain enigmatic.

Authors:
; ; ; ; ; ;
Publication Date:
Research Org.:
Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); National Science Foundation (NSF); Czech Science Foundation; Marie Curie Fellowship
OSTI Identifier:
1547628
Alternate Identifier(s):
OSTI ID: 1607873
Grant/Contract Number:  
FG02-91ER20021; AC02-05CH11231
Resource Type:
Published Article
Journal Name:
Biochimica et Biophysica Acta - Bioenergetics
Additional Journal Information:
Journal Name: Biochimica et Biophysica Acta - Bioenergetics Journal Volume: 1860 Journal Issue: 5; Journal ID: ISSN 0005-2728
Publisher:
Elsevier
Country of Publication:
Netherlands
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; helical carotenoid protein; photoprotection; cyanobacteria; spectroscopic; crystal structure; carotenoid aggregates

Citation Formats

Dominguez-Martin, Maria Agustina, Polívka, Tomáš, Sutter, Markus, Ferlez, Bryan, Lechno-Yossef, Sigal, Montgomery, Beronda L., and Kerfeld, Cheryl A. Structural and spectroscopic characterization of HCP2. Netherlands: N. p., 2019. Web. doi:10.1016/j.bbabio.2019.03.004.
Dominguez-Martin, Maria Agustina, Polívka, Tomáš, Sutter, Markus, Ferlez, Bryan, Lechno-Yossef, Sigal, Montgomery, Beronda L., & Kerfeld, Cheryl A. Structural and spectroscopic characterization of HCP2. Netherlands. doi:10.1016/j.bbabio.2019.03.004.
Dominguez-Martin, Maria Agustina, Polívka, Tomáš, Sutter, Markus, Ferlez, Bryan, Lechno-Yossef, Sigal, Montgomery, Beronda L., and Kerfeld, Cheryl A. Wed . "Structural and spectroscopic characterization of HCP2". Netherlands. doi:10.1016/j.bbabio.2019.03.004.
@article{osti_1547628,
title = {Structural and spectroscopic characterization of HCP2},
author = {Dominguez-Martin, Maria Agustina and Polívka, Tomáš and Sutter, Markus and Ferlez, Bryan and Lechno-Yossef, Sigal and Montgomery, Beronda L. and Kerfeld, Cheryl A.},
abstractNote = {The Helical Carotenoid Proteins (HCPs) are a large group of newly identified carotenoid-binding proteins found in ecophysiologically diverse cyanobacteria. They likely evolved before becoming the effector (quenching) domain of the modular Orange Carotenoid Protein (OCP). The number of discrete HCP families—at least nine—suggests they are involved in multiple distinct functions. Here we report the 1.7 Å crystal structure of HCP2, one of the most widespread HCPs found in nature, from the chromatically acclimating cyanobacterium Tolypothrix sp. PCC 7601. By purifying HCP2 from the native source we are able to identify its natively-bound carotenoid, which is exclusively canthaxanthin. In solution, HCP2 is a monomer with an absorbance maximum of 530 nm. However, the HCP2 crystals have a maximum absorbance at 548 nm, which is accounted by the stacking of the β1 rings of the carotenoid in the two molecules in the asymmetric unit. Our results demonstrate how HCPs provide a valuable system to study carotenoid-protein interactions and their spectroscopic implications, and contribute to efforts to understand the functional roles of this large, newly discovered family of pigment proteins, which to-date remain enigmatic.},
doi = {10.1016/j.bbabio.2019.03.004},
journal = {Biochimica et Biophysica Acta - Bioenergetics},
number = 5,
volume = 1860,
place = {Netherlands},
year = {2019},
month = {5}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
DOI: 10.1016/j.bbabio.2019.03.004

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Cited by: 4 works
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