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PDBsum entry 1sl8
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protein metals links
Luminescent protein PDB id
1sl8

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
181 a.a. *
Metals
_CA ×3
Waters ×154
* Residue conservation analysis
PDB id:
1sl8
Name: Luminescent protein
Title: Calcium-loaded apo-aequorin from aequorea victoria
Structure: Aequorin 1. Chain: a. Engineered: yes
Source: Aequorea victoria. Organism_taxid: 6100. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
1.70Å     R-factor:   0.217     R-free:   0.236
Authors: L.Deng,S.V.Markova,E.S.Vysotski,Z.J.Liu,J.Lee,J.Rose,B.C.Wang, Southeast Collaboratory For Structural Genomics (Secsg)
Key ref:
L.Deng et al. (2005). All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin. Protein Sci, 14, 663-675. PubMed id: 15689515 DOI: 10.1110/ps.041142905
Date:
05-Mar-04     Release date:   28-Dec-04    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P07164  (AEQ1_AEQVI) -  Aequorin-1 from Aequorea victoria
Seq:
Struc: 		196 a.a.
181 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1110/ps.041142905 Protein Sci 14:663-675 (2005)
PubMed id: 15689515  
 
 
All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin.
L.Deng, E.S.Vysotski, S.V.Markova, Z.J.Liu, J.Lee, J.Rose, B.C.Wang.
 
  ABSTRACT  
 
The crystal structures of calcium-loaded apo-aequorin and apo-obelin have been determined at resolutions 1.7A and 2.2 A, respectively. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-protein retain the same compact scaffold and overall fold as the unreacted photoproteins containing the bound substrate, 2-hyroperoxycoelenterazine, and also the same as the Ca2+-discharged obelin bound with product, coleneteramide. Nevertheless, there are easily discerned shifts in both helix and loop regions, and the shifts are not the same between the two proteins. It is suggested that these photoproteins to sense Ca2+ concentration transients and to produce their bioluminescence response on the millisecond timescale. A mechanism of intrastructural transmission of the calcium signal is proposed.
 
  Selected figure(s)  
 
Figure 6.
Hydrogen-bond interactions between helix A and helix H, and helix A and the C terminus in conformation states II and V. (A) Obelin (PDB code1EL4; state II). (B) Aequorin (PDB code 1EJ3, monomer B; state II). (C) Ca^2+-loaded apo-obelin (state V). (D) Ca^2+-loaded apo-aequorin (state V). The photoprotein conformation states II and V are from Figure 1 [triangle] Figure 1.-. The residues for the Ca^2+-loaded apo-aequorin are numbered according to that used for the aequorin structure (PDB code 1EJ3). 		Figure 7.
Stereo view of helix A in conformation states II and V. (A) Obelin (PDB code1EL4; state II). (B) Ca^2+-loaded apo-obelin (state V). (C) Aequorin (PDB code 1EJ3, monomer B; state II). (D) Ca^2+-loaded apo-aequorin (state V). The photoprotein conformation states II and V are from Figure 1 [triangle] Figure 1.-. The residues for the Ca^2+-loaded state of apo-aequorin are numbered according to that used for the aequorin structure (PDB code 1EJ3).
 
  The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (2005, 14, 663-675) copyright 2005.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20003365 T.Liu, and R.B.Altman (2009).
Prediction of calcium-binding sites by combining loop-modeling with machine learning.
  BMC Struct Biol, 9, 72.  
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.  
18385886 G.A.Stepanyuk, Z.J.Liu, S.S.Markova, L.A.Frank, J.Lee, E.S.Vysotski, and B.C.Wang (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.
PDB codes: 2hps 2hq8
18264586 M.S.Titushin, S.V.Markova, L.A.Frank, N.P.Malikova, G.A.Stepanyuk, J.Lee, and E.S.Vysotski (2008).
Coelenterazine-binding protein of Renilla muelleri: cDNA cloning, overexpression, and characterization as a substrate of luciferase.
  Photochem Photobiol Sci, 7, 189-196.  
16769886 L.Tricoire, K.Tsuzuki, O.Courjean, N.Gibelin, G.Bourout, J.Rossier, and B.Lambolez (2006).
Calcium dependence of aequorin bioluminescence dissected by random mutagenesis.
  Proc Natl Acad Sci U S A, 103, 9500-9505.  
16467137 Z.J.Liu, G.A.Stepanyuk, E.S.Vysotski, J.Lee, S.V.Markova, N.P.Malikova, and B.C.Wang (2006).
Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state.
  Proc Natl Acad Sci U S A, 103, 2570-2575.
PDB code: 2f8p
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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