Assembly of photoactive orange carotenoid protein from its domains unravels a carotenoid shuttle mechanism.
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The Unique Protein-to-Protein Carotenoid Transfer Mechanism.The photocycle of orange carotenoid protein conceals distinct intermediates and asynchronous changes in the carotenoid and protein components.Engineering a carotenoid-binding site in Dokdonia sp. PRO95 Na(+)-translocating rhodopsin by a single amino acid substitution.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.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
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P2860
Assembly of photoactive orange carotenoid protein from its domains unravels a carotenoid shuttle mechanism.
description
2017 nî lūn-bûn
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2017年の論文
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年学术文章
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name
Assembly of photoactive orange ...... carotenoid shuttle mechanism.
@en
Assembly of photoactive orange ...... carotenoid shuttle mechanism.
@nl
type
label
Assembly of photoactive orange ...... carotenoid shuttle mechanism.
@en
Assembly of photoactive orange ...... carotenoid shuttle mechanism.
@nl
prefLabel
Assembly of photoactive orange ...... carotenoid shuttle mechanism.
@en
Assembly of photoactive orange ...... carotenoid shuttle mechanism.
@nl
P2093
P2860
P50
P1476
Assembly of photoactive orange ...... carotenoid shuttle mechanism.
@en
P2093
David Buhrke
Franz-Josef Schmitt
Neslihan N Tavraz
Thomas Friedrich
P2860
P2888
P304
P356
10.1007/S11120-017-0353-3
P577
2017-02-17T00:00:00Z