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PDBsum entry 4nxg
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Flavoprotein, fluorescent protein
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PDB id
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4nxg
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PDB id:
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| Name: |
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Flavoprotein, fluorescent protein
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Title:
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Crystal structure of ilov-i486z(2lt) at ph 9.0
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Structure:
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Phototropin-2. Chain: a, b. Fragment: lov domain, unp residues 388-496. Synonym: defective in chloroplast avoidance protein 1, non- phototropic hypocotyl 1-like protein 1, atkin7, nph1-like protein 1. Engineered: yes. Mutation: yes
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Source:
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Arabidopsis thaliana. Mouse-ear cress, thale-cress. Organism_taxid: 3702. Gene: phot2, cav1, kin7, npl1, at5g58140, k21l19.6. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.09Å
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R-factor:
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0.199
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R-free:
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0.229
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Authors:
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J.Wang,X.Liu,J.Li
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Key ref:
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X.Liu
et al.
(2014).
Significant expansion of fluorescent protein sensing ability through the genetic incorporation of superior photo-induced electron-transfer quenchers.
J Am Chem Soc,
136,
13094-13097.
PubMed id:
DOI:
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Date:
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09-Dec-13
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Release date:
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24-Sep-14
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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.
103 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 7 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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J Am Chem Soc
136:13094-13097
(2014)
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PubMed id:
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Significant expansion of fluorescent protein sensing ability through the genetic incorporation of superior photo-induced electron-transfer quenchers.
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X.Liu,
L.Jiang,
J.Li,
L.Wang,
Y.Yu,
Q.Zhou,
X.Lv,
W.Gong,
Y.Lu,
J.Wang.
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ABSTRACT
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Photo-induced electron transfer (PET) is ubiquitous for photosynthesis and
fluorescent sensor design. However, genetically coded PET sensors are
underdeveloped, due to the lack of methods to site-specifically install PET
probes on proteins. Here we describe a family of acid and Mn(III) turn-on
fluorescent protein (FP) sensors, named iLovU, based on PET and the genetic
incorporation of superior PET quenchers in the fluorescent flavoprotein iLov.
Using the iLovU PET sensors, we monitored the cytoplasmic acidification process,
and achieved Mn(III) fluorescence sensing for the first time. The iLovU sensors
should be applicable for studying pH changes in living cells, monitoring
biogentic Mn(III) in the environment, and screening for efficient manganese
peroxidase, which is highly desirable for lignin degradation and biomass
conversion. Our work establishes a platform for many more protein PET sensors,
facilitates the de novo design of metalloenzymes harboring redox active
residues, and expands our ability to probe protein conformational dynamics.
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