Structural and functional modularity of the orange carotenoid protein: distinct roles for the N- and C-terminal domains in cyanobacterial photoprotection.
about
Biosynthesis of soluble carotenoid holoproteins in Escherichia coli.Local and global structural drivers for the photoactivation of the orange carotenoid protein.Synthetic OCP heterodimers are photoactive and recapitulate the fusion of two primitive carotenoproteins in the evolution of cyanobacterial photoprotection.Isotope-Encoded Carboxyl Group Footprinting for Mass Spectrometry-Based Protein Conformational StudiesOrange carotenoid protein burrows into the phycobilisome to provide photoprotectionNative mass spectrometry and ion mobility characterize the orange carotenoid protein functional domainsModulating energy arriving at photochemical reaction centers: orange carotenoid protein-related photoprotection and state transitions.A comparative study of three signaling forms of the orange carotenoid protein.Dramatic Domain Rearrangements of the Cyanobacterial Orange Carotenoid Protein upon Photoactivation.The Signaling State of Orange Carotenoid Protein.Discovery of carotenoid red-shift in endolithic cyanobacteria from the Atacama Desert.Different Functions of the Paralogs to the N-Terminal Domain of the Orange Carotenoid Protein in the Cyanobacterium Anabaena sp. PCC 7120.Additional families of orange carotenoid proteins in the photoprotective system of cyanobacteria.The Unique Protein-to-Protein Carotenoid Transfer Mechanism.Assembly of photoactive orange carotenoid protein from its domains unravels a carotenoid shuttle mechanism.Role of inter-domain cavity in the attachment of the orange carotenoid protein to the phycobilisome core and to the fluorescence recovery protein.The photocycle of orange carotenoid protein conceals distinct intermediates and asynchronous changes in the carotenoid and protein components.Paralogs of the C-Terminal Domain of the Cyanobacterial Orange Carotenoid Protein Are Carotenoid Donors to Helical Carotenoid Proteins.A Molecular Mechanism for Nonphotochemical Quenching in Cyanobacteria.Interaction of the signaling state analog and the apoprotein form of the orange carotenoid protein with the fluorescence recovery protein.Regulation of Orange Carotenoid Protein Activity in Cyanobacterial Photoprotection.Photoactivation and relaxation studies on the cyanobacterial orange carotenoid protein in the presence of copper ion.Fluorescent Labeling Preserving OCP Photoactivity Reveals Its Reorganization during the Photocycle.Chemical activation of the cyanobacterial orange carotenoid protein.Deletion of the short N-terminal extension in OCP reveals the main site for FRP binding.Structural rearrangements in the C-terminal domain homolog of Orange Carotenoid Protein are crucial for carotenoid transferOCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria
P2860
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P2860
Structural and functional modularity of the orange carotenoid protein: distinct roles for the N- and C-terminal domains in cyanobacterial photoprotection.
description
2014 nî lūn-bûn
@nan
2014年の論文
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2014年学术文章
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2014年学术文章
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2014年学术文章
@zh-cn
2014年学术文章
@zh-hans
2014年学术文章
@zh-my
2014年学术文章
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2014年學術文章
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name
Structural and functional modu ...... yanobacterial photoprotection.
@en
Structural and functional modu ...... yanobacterial photoprotection.
@nl
type
label
Structural and functional modu ...... yanobacterial photoprotection.
@en
Structural and functional modu ...... yanobacterial photoprotection.
@nl
prefLabel
Structural and functional modu ...... yanobacterial photoprotection.
@en
Structural and functional modu ...... yanobacterial photoprotection.
@nl
P2093
P2860
P356
P1433
P1476
Structural and functional modu ...... yanobacterial photoprotection.
@en
P2093
Cheryl A Kerfeld
Ming-De Li
Richard A Mathies
Ryan L Leverenz
P2860
P304
P356
10.1105/TPC.113.118588
P577
2014-01-07T00:00:00Z