PDBsum entry 2hq8

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protein metals Protein-protein interface(s) links
Structural genomics, unknown function PDB id
Protein chains
181 a.a. *
_CA ×6
Waters ×300
* Residue conservation analysis
PDB id:
Name: Structural genomics, unknown function
Title: Crystal structure of coelenterazine-binding protein from renilla muelleri in the ca loaded apo form
Structure: Coelenterazine-binding protein ca-bound apo form. Chain: a, b. Engineered: yes
Source: Renilla muelleri. Organism_taxid: 37510. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: bl21.
1.80Å     R-factor:   0.207     R-free:   0.247
Authors: G.Stepanyuk,Z.J.Liu,E.S.Vysotski,J.Lee,J.P.Rose,B.C.Wang, Southeast Collaboratory For Structural Genomics (Secsg)
Key ref: G.A.Stepanyuk et al. (2008). Crystal structure of coelenterazine-binding protein from Renilla muelleri at 1.7 A: why it is not a calcium-regulated photoprotein. Photochem Photobiol Sci, 7, 442-447. PubMed id: 18385886
18-Jul-06     Release date:   12-Sep-06    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
C9V488  (C9V488_RENMU) -  Ca2+-triggered coelenterazine-binding protein 1
186 a.a.
181 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     metal ion binding     2 terms  


Photochem Photobiol Sci 7:442-447 (2008)
PubMed id: 18385886  
Crystal structure of coelenterazine-binding protein from Renilla muelleri at 1.7 A: why it is not a calcium-regulated photoprotein.
G.A.Stepanyuk, Z.J.Liu, S.S.Markova, L.A.Frank, J.Lee, E.S.Vysotski, B.C.Wang.
Bioluminescence in the sea pansy Renilla involves two distinct proteins, a Ca2+-triggered coelenterazine-binding protein (CBP), and Renilla luciferase. CBP contains one tightly bound coelenterazine molecule, which becomes available for reaction with luciferase and O2 only subsequent to Ca2+ binding. CBP belongs to the EF-hand superfamily of Ca2+-binding proteins and contains three "EF-hand" Ca2+-binding sites. The overall spatial structure of recombinant selenomethionine-labeled CBP determined at 1.7 A, is found to approximate the protein scaffold characteristic of the class of Ca2+-regulated photoproteins. Photoproteins however, catalyze molecular oxygen addition to coelenterazine producing a 2-hydroperoxycoelenterazine intermediate, which is stabilized within the binding cavity in the absence of Ca2+. Addition of Ca2+ triggers the bioluminescence reaction. However in CBP this first step of oxygen addition is not allowed. The different amino acid environments and hydrogen bond interactions within the binding cavity, are proposed to account for the different properties of the two classes of proteins.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20711766 G.A.Stepanyuk, J.Unch, N.P.Malikova, S.V.Markova, J.Lee, and E.S.Vysotski (2010).
Coelenterazine-v ligated to Ca2+-triggered coelenterazine-binding protein is a stable and efficient substrate of the red-shifted mutant of Renilla muelleri luciferase.
  Anal Bioanal Chem, 398, 1809-1817.  
18655070 G.A.Stepanyuk, Z.J.Liu, E.S.Vysotski, J.Lee, J.P.Rose, and B.C.Wang (2009).
Structure based mechanism of the Ca(2+)-induced release of coelenterazine from the Renilla binding protein.
  Proteins, 74, 583-593.  
18595733 G.A.Stepanyuk, H.Xu, C.K.Wu, S.V.Markova, J.Lee, E.S.Vysotski, and B.C.Wang (2008).
Expression, purification and characterization of the secreted luciferase of the copepod Metridia longa from Sf9 insect cells.
  Protein Expr Purif, 61, 142-148.  
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