Biomolecular NMR Assignments, volume 15, issue 1, pages 17-23

NMR resonance assignment and backbone dynamics of a C-terminal domain homolog of orange carotenoid protein

Maksimov Eugene G 1, 2, 3
Laptev Gennady Yu 1
Blokhin Dmitriy S 4
Klochkov Vladimir V 4
Slonimskiy Yury B. 2
Friedrich Thomas 5
Chang Chi-Fon 6
Publication typeJournal Article
Publication date2020-09-16
Quartile SCImago
Q3
Quartile WOS
Q4
Impact factor0.9
ISSN18742718, 1874270X
Biochemistry
Structural Biology
Abstract
Photoprotection in cyanobacteria is mediated by the Orange Carotenoid Protein (OCP), a two-domain photoswitch which has multiple natural homologs of its N- and C-terminal domains. Recently, it was demonstrated that C-terminal domain homologs (CTDHs) of OCP are standalone carotenoproteins participating in multidirectional carotenoid transfer between membranes and proteins. Non-covalent embedment of a ketocarotenoid causes dimerization of the small 16-kDa water-soluble CTDH protein; however, dynamic interactions of CTDH with membranes and other proteins apparently require the monomeric state. Although crystallography recently provided static snapshots of the Anabaena CTDH (AnaCTDH) spatial structure in the apo-form, which predicted mobility of some putative functional segments, no crystallographic information on the holo-form of CTDH is presently available. In order to use NMR techniques to cope with the dynamics of the AnaCTDH protein, it was necessary to obtain 1H, 13C and 15N resonance assignments. AnaCTDH samples enriched with 13C and 15N isotopes were prepared using recombinant protein expression, and NMR resonance assignment was achieved for more than 90% of the residues. The obtained results revealed that the structure of AnaCTDH in solution and in the crystal are largely equivalent. Together with 15N NMR relaxation experiments, our data shed light on the AnaCTDH dynamics and provide the platform for the subsequent analysis of the holo-CTDH structure in solution, for the better understanding of light-triggered protein-protein interactions and the development of antioxidant nanocarriers for biomedical applications in the future.

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Maksimov E. G. et al. NMR resonance assignment and backbone dynamics of a C-terminal domain homolog of orange carotenoid protein // Biomolecular NMR Assignments. 2020. Vol. 15. No. 1. pp. 17-23.
GOST all authors (up to 50) Copy
Maksimov E. G., Laptev G. Yu., Blokhin D. S., Klochkov V. V., Slonimskiy Y. B., Sluchanko N. N., Friedrich T., Chang C., Polshakov V. I. NMR resonance assignment and backbone dynamics of a C-terminal domain homolog of orange carotenoid protein // Biomolecular NMR Assignments. 2020. Vol. 15. No. 1. pp. 17-23.
RIS |
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TY - JOUR
DO - 10.1007/s12104-020-09976-1
UR - https://doi.org/10.1007%2Fs12104-020-09976-1
TI - NMR resonance assignment and backbone dynamics of a C-terminal domain homolog of orange carotenoid protein
T2 - Biomolecular NMR Assignments
AU - Laptev, Gennady Yu
AU - Blokhin, Dmitriy S
AU - Slonimskiy, Yury B.
AU - Friedrich, Thomas
AU - Chang, Chi-Fon
AU - Polshakov, Vladimir I.
AU - Maksimov, Eugene G
AU - Klochkov, Vladimir V
AU - Sluchanko, Nikolai N
PY - 2020
DA - 2020/09/16 00:00:00
PB - Springer Nature
SP - 17-23
IS - 1
VL - 15
SN - 1874-2718
SN - 1874-270X
ER -
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@article{2020_Maksimov,
author = {Gennady Yu Laptev and Dmitriy S Blokhin and Yury B. Slonimskiy and Thomas Friedrich and Chi-Fon Chang and Vladimir I. Polshakov and Eugene G Maksimov and Vladimir V Klochkov and Nikolai N Sluchanko},
title = {NMR resonance assignment and backbone dynamics of a C-terminal domain homolog of orange carotenoid protein},
journal = {Biomolecular NMR Assignments},
year = {2020},
volume = {15},
publisher = {Springer Nature},
month = {sep},
url = {https://doi.org/10.1007%2Fs12104-020-09976-1},
number = {1},
pages = {17--23},
doi = {10.1007/s12104-020-09976-1}
}
MLA
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Maksimov, Eugene G., et al. “NMR resonance assignment and backbone dynamics of a C-terminal domain homolog of orange carotenoid protein.” Biomolecular NMR Assignments, vol. 15, no. 1, Sep. 2020, pp. 17-23. https://doi.org/10.1007%2Fs12104-020-09976-1.
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