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PDBsum entry 6abh

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protein Protein-protein interface(s) links
Luminescent protein PDB id
6abh

 

 

 

 

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Contents
Protein chains
377 a.a.
(+ 0 more) 405 a.a.
442 a.a.
PDB id:
6abh
Name: Luminescent protein
Title: Structure of a natural red emitting luciferase from phrixothrix hirtus (p1 crystal form)
Structure: Red-bioluminescence eliciting luciferase. Chain: a, b, c, d, e, f, g, h. Engineered: yes
Source: Phrixothrix hirtus. Organism_taxid: 94779. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Resolution:
3.05Å     R-factor:   0.241     R-free:   0.285
Authors: C.Carrasco-Lopez,S.Panjikar,P.Naumov,W.Rabeh
Key ref: C.Carrasco-López et al. (2018). Beetle luciferases with naturally red- and blue-shifted emission. Life Sci Alliance, 1, e201800072. PubMed id: 30456363
Date:
21-Jul-18     Release date:   22-Aug-18    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9U4U7  (Q9U4U7_9COLE) -  Luciferin 4-monooxygenase from Phrixothrix hirtus
Seq:
Struc:
 
Seq:
Struc:
546 a.a.
377 a.a.
Protein chains
Pfam   ArchSchema ?
Q9U4U7  (Q9U4U7_9COLE) -  Luciferin 4-monooxygenase from Phrixothrix hirtus
Seq:
Struc:
 
Seq:
Struc:
546 a.a.
405 a.a.
Protein chain
Pfam   ArchSchema ?
Q9U4U7  (Q9U4U7_9COLE) -  Luciferin 4-monooxygenase from Phrixothrix hirtus
Seq:
Struc:
 
Seq:
Struc:
546 a.a.
442 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E, F, G, H: E.C.1.13.12.7  - firefly luciferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Photinus-luciferin 4-monooxygenase (ATP-hydrolysing)
      Reaction: firefly D-luciferin + ATP + O2 = firefly oxyluciferin + hnu + AMP + CO2 + diphosphate
firefly D-luciferin
+ ATP
+ O2
= firefly oxyluciferin
+ hnu
+ AMP
+ CO2
+ diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Life Sci Alliance 1:e201800072 (2018)
PubMed id: 30456363  
 
 
Beetle luciferases with naturally red- and blue-shifted emission.
C.Carrasco-López, J.C.Ferreira, N.M.Lui, S.Schramm, R.Berraud-Pache, I.Navizet, S.Panjikar, P.Naumov, W.M.Rabeh.
 
  ABSTRACT  
 
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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