Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F20%3A43901339" target="_blank" >RIV/60076658:12310/20:43901339 - isvavai.cz</a>

Result on the web

<a href="https://www.nature.com/articles/s41598-020-72383-y" target="_blank" >https://www.nature.com/articles/s41598-020-72383-y</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41598-020-72383-y" target="_blank" >10.1038/s41598-020-72383-y</a>

Result language

angličtina

Original language name

Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP

Original language description

The Orange Carotenoid Protein (OCP) is a water-soluble protein that governs photoprotection in many cyanobacteria. The 35 kDa OCP is structurally and functionally modular, consisting of an N-terminal effector domain (NTD) and a C-terminal regulatory domain (CTD); a carotenoid spans the two domains. The CTD is a member of the ubiquitous Nuclear Transport Factor-2 (NTF2) superfamily (pfam02136). With the increasing availability of cyanobacterial genomes, bioinformatic analysis has revealed the existence of a new family of proteins, homologs to the CTD, the C-terminal domain-like carotenoid proteins (CCPs). Here we purify holo-CCP2 directly from cyanobacteria and establish that it natively binds canthaxanthin (CAN). We use small-angle X-ray scattering (SAXS) to characterize the structure of this carotenoprotein in two distinct oligomeric states. A single carotenoid molecule spans the two CCPs in the dimer. Our analysis with X-ray footprinting-mass spectrometry (XFMS) identifies critical residues for carotenoid binding that likely contribute to the extreme red shift (ca. 80 nm) of the absorption maximum of the carotenoid bound by the CCP2 dimer and a further 10 nm shift in the tetramer form. These data provide the first structural description of carotenoid binding by a protein consisting of only an NTF2 domain.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10610 - Biophysics

Project

<a href="/en/project/GA18-21631S" target="_blank" >GA18-21631S: Ultrafast spectroscopy as a tool for elucidation the structure-function relationship in cyanobacterial carotenoid-binding proteins</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2020

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Scientific Reports

ISSN

2045-2322

e-ISSN

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Volume of the periodical

10

Issue of the periodical within the volume

1

Country of publishing house

GB - UNITED KINGDOM

Number of pages

11

Pages from-to

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UT code for WoS article

000573849300092

EID of the result in the Scopus database

2-s2.0-85091420678