Crystal structure of the FRP and identification of the active site for modulation of OCP-mediated photoprotection in cyanobacteria
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PHOTOSYNTHESIS. A 12 Å carotenoid translocation in a photoswitch associated with cyanobacterial photoprotectionResolving the contribution of the uncoupled phycobilisomes to cyanobacterial pulse-amplitude modulated (PAM) fluorometry signals.Activated OCP unlocks nonphotochemical quenching in cyanobacteriaLocal 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.Orange carotenoid protein burrows into the phycobilisome to provide photoprotectionMolecular mechanism of photoactivation and structural location of the cyanobacterial orange carotenoid protein.Modulating energy arriving at photochemical reaction centers: orange carotenoid protein-related photoprotection and state transitions.Dramatic Domain Rearrangements of the Cyanobacterial Orange Carotenoid Protein upon Photoactivation.The Signaling State of Orange Carotenoid Protein.Electronic coupling of the phycobilisome with the orange carotenoid protein and fluorescence quenching.Specificity of the cyanobacterial orange carotenoid protein: influences of orange carotenoid protein and phycobilisome structures.Additional families of orange carotenoid proteins in the photoprotective system of cyanobacteria.Structural and functional modularity of the orange carotenoid protein: distinct roles for the N- and C-terminal domains in cyanobacterial photoprotection.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.Photoactivation mechanism of a carotenoid-based photoreceptor.A Molecular Mechanism for Nonphotochemical Quenching in Cyanobacteria.Native Mass Spectrometry Analysis of Oligomerization States of Fluorescence Recovery Protein and Orange Carotenoid Protein: Two Proteins Involved in the Cyanobacterial Photoprotection Cycle.Photoprotective, excited-state quenching mechanisms in diverse photosynthetic organisms.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.Features of temporal behavior of fluorescence recovery in Synechocystis sp. PCC6803.Deletion of the short N-terminal extension in OCP reveals the main site for FRP binding.Biophysical modeling of in vitro and in vivo processes underlying regulated photoprotective mechanism in cyanobacteria.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
Crystal structure of the FRP and identification of the active site for modulation of OCP-mediated photoprotection in cyanobacteria
description
2013 nî lūn-bûn
@nan
2013 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Crystal structure of the FRP a ...... otoprotection in cyanobacteria
@ast
Crystal structure of the FRP a ...... otoprotection in cyanobacteria
@en
Crystal structure of the FRP a ...... otoprotection in cyanobacteria
@nl
type
label
Crystal structure of the FRP a ...... otoprotection in cyanobacteria
@ast
Crystal structure of the FRP a ...... otoprotection in cyanobacteria
@en
Crystal structure of the FRP a ...... otoprotection in cyanobacteria
@nl
prefLabel
Crystal structure of the FRP a ...... otoprotection in cyanobacteria
@ast
Crystal structure of the FRP a ...... otoprotection in cyanobacteria
@en
Crystal structure of the FRP a ...... otoprotection in cyanobacteria
@nl
P2093
P2860
P50
P356
P1476
Crystal structure of the FRP a ...... otoprotection in cyanobacteria
@en
P2093
Annette E Salmeen
Cheryl A Kerfeld
Ryan L Leverenz
P2860
P304
10022-10027
P356
10.1073/PNAS.1303673110
P407
P577
2013-05-28T00:00:00Z