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PDBsum entry 6gpu
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PDB id:
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Flavoprotein
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Title:
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Crystal structure of minisog at 1.17a resolution
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Structure:
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Phototropin-2. Chain: a. Synonym: defective in chloroplast avoidance protein 1,non-phototropic hypocotyl 1-like protein 1,nph1-like protein 1. Engineered: yes. Other_details: efipnpllg
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Source:
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Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: phot2, cav1, kin7, npl1, at5g58140, k21l19.6. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693
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Resolution:
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1.17Å
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R-factor:
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0.134
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R-free:
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0.164
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Authors:
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C.Lafaye,L.Signor,S.Aumonier,X.Shu,G.Gotthard,A.Royant
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Key ref:
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J.Torra
et al.
(2019).
Tailing miniSOG: structural bases of the complex photophysics of a flavin-binding singlet oxygen photosensitizing protein.
Sci Rep,
9,
2428.
PubMed id:
DOI:
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Date:
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07-Jun-18
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Release date:
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27-Feb-19
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PROCHECK
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Headers
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References
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P93025
(PHOT2_ARATH) -
Phototropin-2 from Arabidopsis thaliana
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Seq:
Struc:
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915 a.a.
115 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 13 residue positions (black
crosses)
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Enzyme class:
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E.C.2.7.11.1
- non-specific serine/threonine protein kinase.
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Reaction:
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1.
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L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
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2.
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
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L-seryl-[protein]
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+
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ATP
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=
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O-phospho-L-seryl-[protein]
Bound ligand (Het Group name = )
matches with 61.11% similarity
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+
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ADP
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+
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H(+)
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L-threonyl-[protein]
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+
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ATP
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=
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O-phospho-L-threonyl-[protein]
Bound ligand (Het Group name = )
matches with 61.11% similarity
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Sci Rep
9:2428
(2019)
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PubMed id:
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Tailing miniSOG: structural bases of the complex photophysics of a flavin-binding singlet oxygen photosensitizing protein.
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J.Torra,
C.Lafaye,
L.Signor,
S.Aumonier,
C.Flors,
X.Shu,
S.Nonell,
G.Gotthard,
A.Royant.
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ABSTRACT
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miniSOG is the first flavin-binding protein that has been developed with the
specific aim of serving as a genetically-encodable light-induced source of
singlet oxygen (1O2). We have determined its 1.17 Å
resolution structure, which has allowed us to investigate its mechanism of
photosensitization using an integrated approach combining spectroscopic and
structural methods. Our results provide a structural framework to explain the
ability of miniSOG to produce 1O2 as a competition between
oxygen- and protein quenching of its triplet state. In addition, a third
excited-state decay pathway has been identified that is pivotal for the
performance of miniSOG as 1O2 photosensitizer, namely the
photo-induced transformation of flavin mononucleotide (FMN) into lumichrome,
which increases the accessibility of oxygen to the flavin FMN chromophore and
makes protein quenching less favourable. The combination of the two effects
explains the increase in the 1O2 quantum yield by one
order of magnitude upon exposure to blue light. Besides, we have identified
several surface electron-rich residues that are progressively photo-oxidized,
further contributing to facilitate the production of 1O2.
Our results help reconcile the apparent poor level of 1O2
generation by miniSOG and its excellent performance in correlative light and
electron microscopy experiments.
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Links
