PDBsum entry 2hps

Luminescent protein

PDB id

2hps

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Contents

			Protein chain

					184 a.a. *

			Ligands

					CTZ


					GOL ×2

			Waters ×176

* Residue conservation analysis

PDB id:

2hps

Links

Name:

Luminescent protein

Title:

Crystal structure of coelenterazine-binding protein from renilla muelleri

Structure:

Coelenterazine-binding protein with bound coelenterazine. Chain: a. Engineered: yes

Source:

Renilla muelleri. Organism_taxid: 37510. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Resolution:

1.72Å

R-factor:

0.200

R-free:

0.229

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

Date:

17-Jul-06

Release date:

09-Jan-07

PROCHECK

	Headers

	References

Protein chain

C9V488 (C9V488_RENMU) - Ca2+-triggered coelenterazine-binding protein 1 from Renilla muelleri

Seq: Struc:					186 a.a. 184 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

	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.

ABSTRACT

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.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.