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PDBsum entry 6abh
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Luminescent protein
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PDB id
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6abh
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Contents |
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377 a.a.
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(+ 0 more)
405 a.a.
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442 a.a.
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PDB id:
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| Name: |
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Luminescent protein
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Title:
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Structure of a natural red emitting luciferase from phrixothrix hirtus (p1 crystal form)
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Structure:
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Red-bioluminescence eliciting luciferase. Chain: a, b, c, d, e, f, g, h. Engineered: yes
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Source:
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Phrixothrix hirtus. Organism_taxid: 94779. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
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Resolution:
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3.05Å
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R-factor:
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0.241
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R-free:
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0.285
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Authors:
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C.Carrasco-Lopez,S.Panjikar,P.Naumov,W.Rabeh
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Key ref:
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C.Carrasco-López
et al.
(2018).
Beetle luciferases with naturally red- and blue-shifted emission.
Life Sci Alliance,
1,
e201800072.
PubMed id:
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Date:
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21-Jul-18
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Release date:
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22-Aug-18
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PROCHECK
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Headers
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References
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Q9U4U7
(Q9U4U7_9COLE) -
Luciferin 4-monooxygenase from Phrixothrix hirtus
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Seq: Struc:
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546 a.a.
377 a.a.
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Enzyme class:
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Chains A, B, C, D, E, F, G, H:
E.C.1.13.12.7
- firefly luciferase.
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Pathway:
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Photinus-luciferin 4-monooxygenase (ATP-hydrolysing)
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Reaction:
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firefly D-luciferin + ATP + O2 = firefly oxyluciferin + hnu + AMP + CO2 + diphosphate
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firefly D-luciferin
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ATP
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O2
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=
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firefly oxyluciferin
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hnu
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+
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AMP
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CO2
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diphosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Life Sci Alliance
1:e201800072
(2018)
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PubMed id:
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Beetle luciferases with naturally red- and blue-shifted emission.
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C.Carrasco-López,
J.C.Ferreira,
N.M.Lui,
S.Schramm,
R.Berraud-Pache,
I.Navizet,
S.Panjikar,
P.Naumov,
W.M.Rabeh.
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ABSTRACT
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The different colors of light emitted by bioluminescent beetles that use an
identical substrate and chemiexcitation reaction sequence to generate light
remain a challenging and controversial mechanistic conundrum. The crystal
structures of two beetle luciferases with red- and blue-shifted light relative
to the green yellow light of the common firefly species provide direct insight
into the molecular origin of the bioluminescence color. The structure of a
blue-shifted green-emitting luciferase from the firefly Amydetes vivianii
is monomeric with a structural fold similar to the previously reported firefly
luciferases. The only known naturally red-emitting luciferase from the glow-worm
Phrixothrix hirtus exists as tetramers and octamers. Structural and
computational analyses reveal varying aperture between the two domains enclosing
the active site. Mutagenesis analysis identified two conserved loops that
contribute to the color of the emitted light. These results are expected to
advance comparative computational studies into the conformational landscape of
the luciferase reaction sequence.
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');
}
}
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