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PDBsum entry 2fqe
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protein ligands metals links
Oxidoreductase PDB id
2fqe

 

 

 

 

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Contents
Protein chain
463 a.a. *
Ligands
C2O
CIT
Metals
_CU ×2
_NA
Waters ×416
* Residue conservation analysis
PDB id:
2fqe
Name: Oxidoreductase
Title: Crystal structures of e. Coli laccase cueo under different copper binding situations
Structure: Blue copper oxidase cueo. Chain: a. Synonym: laccase cueo, copper efflux oxidase. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562
Resolution:
1.92Å     R-factor:   0.165     R-free:   0.205
Authors: X.Li,Z.Wei,M.Zhang,M.Teng,W.Gong
Key ref: X.Li et al. (2007). Crystal structures of E. coli laccase CueO at different copper concentrations. Biochem Biophys Res Commun, 354, 21-26. PubMed id: 17217912
Date:
18-Jan-06     Release date:   30-Jan-07    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P36649  (CUEO_ECOLI) -  Multicopper oxidase CueO from Escherichia coli (strain K12)
Seq:
Struc: 		516 a.a.
463 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.16.3.4  - cuproxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 4 Cu+ + O2 + 4 H+ = 4 Cu2+ + 2 H2O
4 × Cu(+)
 + O2
 + 4 × H(+)
 = 4 × Cu(2+)
 + 2 × H2O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Key reference    
 
 
Biochem Biophys Res Commun 354:21-26 (2007)
PubMed id: 17217912  
 
 
Crystal structures of E. coli laccase CueO at different copper concentrations.
X.Li, Z.Wei, M.Zhang, X.Peng, G.Yu, M.Teng, W.Gong.
 
  ABSTRACT  
 
CueO protein is a hypothetical bacterial laccase and a good laccase candidate for large scale industrial application. Four CueO crystal structures were determined at different copper concentrations. Low copper occupancy in apo-CueO and slow copper reconstitution process in CueO with exogenous copper were demonstrated. These observations well explain the copper dependence of CueO oxidase activity. Structural comparison between CueO and other three fungal laccase proteins indicates that Glu106 in CueO constitutes the primary counter-work for reconstitution of the trinuclear copper site. Mutation of Glu106 to a Phe enhanced CueO oxidation activity and supported this hypothesis. In addition, an extra alpha-helix from Leu351 to Gly378 covers substrate biding pocket of CueO and might compromises the electron transfer from substrate to type I copper.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21120471 J.Zeng, X.Lin, J.Zhang, X.Li, and M.H.Wong (2011).
Oxidation of polycyclic aromatic hydrocarbons by the bacterial laccase CueO from E. coli.
  Appl Microbiol Biotechnol, 89, 1841-1849.  
21076916 X.Liu, M.Gillespie, A.D.Ozel, E.Dikici, S.Daunert, and L.G.Bachas (2011).
Electrochemical properties and temperature dependence of a recombinant laccase from Thermus thermophilus.
  Anal Bioanal Chem, 399, 361-366.  
20473548 M.Mohammadian, M.Fathi-Roudsari, N.Mollania, A.Badoei-Dalfard, and K.Khajeh (2010).
Enhanced expression of a recombinant bacterial laccase at low temperature and microaerobic conditions: purification and biochemical characterization.
  J Ind Microbiol Biotechnol, 37, 863-869.  
20200715 Z.Chen, P.Durão, C.S.Silva, M.M.Pereira, S.Todorovic, P.Hildebrandt, I.Bento, P.F.Lindley, and L.O.Martins (2010).
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis.
  Dalton Trans, 39, 2875-2882.
PDB codes: 4ako 4akp 4akq
19034452 C.Pezzella, F.Autore, P.Giardina, A.Piscitelli, G.Sannia, and V.Faraco (2009).
The Pleurotus ostreatus laccase multi-gene family: isolation and heterologous expression of new family members.
  Curr Genet, 55, 45-57.  
19236694 K.Koschorreck, R.D.Schmid, and V.B.Urlacher (2009).
Improving the functional expression of a Bacillus licheniformis laccase by random and site-directed mutagenesis.
  BMC Biotechnol, 9, 12.  
18330561 K.Koschorreck, S.M.Richter, A.B.Ene, E.Roduner, R.D.Schmid, and V.B.Urlacher (2008).
Cloning and characterization of a new laccase from Bacillus licheniformis catalyzing dimerization of phenolic acids.
  Appl Microbiol Biotechnol, 79, 217-224.  
18772935 Y.Li, J.Yin, G.Qu, L.Lv, Y.Li, S.Yang, and X.G.Wang (2008).
Gene cloning, protein purification, and enzymatic properties of multicopper oxidase, from Klebsiella sp. 601.
  Can J Microbiol, 54, 725-733.  
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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