spacer
spacer
Go to PDB code: 
protein metals Protein-protein interface(s) links
Oxidoreductase PDB id
1ivv
Jmol
Contents
Protein chains
620 a.a. *
Metals
_CU ×2
Waters ×1213
* Residue conservation analysis
PDB id:
1ivv
Name: Oxidoreductase
Title: Crystal structure of copper amine oxidase from arthrobacter globiformis: early intermediate in topaquinone biogenesis
Structure: Amine oxidase. Chain: a, b. Synonym: phenylethylamine oxidase. Engineered: yes
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
2.10Å     R-factor:   0.190     R-free:   0.263
Authors: M.Kim,T.Okajima,S.Kishishita,M.Yoshimura,A.Kawamori,K.Taniza H.Yamaguchi
Key ref:
M.Kim et al. (2002). X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase. Nat Struct Biol, 9, 591-596. PubMed id: 12134140 DOI: 10.1038/nsb824
Date:
29-Mar-02     Release date:   07-Aug-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P46881  (PAOX_ARTGO) -  Phenylethylamine oxidase
Seq:
Struc: 		 
Seq:
Struc: 		638 a.a.
620 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.1.4.3.21  - Primary-amine oxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
RCH(2)NH(2)
 + H(2)O
 + O(2)
 = RCHO
 + NH(3)
 + H(2)O(2)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     tryptamine:oxygen oxidoreductase (deaminating) activity     9 terms  

 

 
    reference    
 
 
DOI no: 10.1038/nsb824 Nat Struct Biol 9:591-596 (2002)
PubMed id: 12134140  
 
 
X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase.
M.Kim, T.Okajima, S.Kishishita, M.Yoshimura, A.Kawamori, K.Tanizawa, H.Yamaguchi.
 
  ABSTRACT  
 
The quinone cofactor TPQ in copper amine oxidase is generated by posttranslational modification of an active site tyrosine residue. Using X-ray crystallography, we have probed the copper-dependent autooxidation process of TPQ in the enzyme from Arthrobacter globiformis. Apo enzyme crystals were anaerobically soaked with copper; the structure determined from this crystal provides a view of the initial state: the unmodified tyrosine coordinated to the bound copper. Exposure of the copper-bound crystals to oxygen led to the formation of freeze-trapped intermediates; structural analyses indicate that these intermediates contain dihydroxyphenylalanine quinone and trihydroxyphenylalanine. These are the first visualized intermediates during TPQ biogenesis in copper amine oxidase.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21169693 M.Kataoka, H.Oya, A.Tominaga, M.Otsu, T.Okajima, K.Tanizawa, and H.Yamaguchi (2011).
Detection of the reaction intermediates catalyzed by a copper amine oxidase.
  J Synchrotron Radiat, 18, 58-61.  
20936199 V.L.Davidson (2011).
Generation of protein-derived redox cofactors by posttranslational modification.
  Mol Biosyst, 7, 29-37.  
20645325 E.Cremades, J.Echeverría, and S.Alvarez (2010).
The trigonal prism in coordination chemistry.
  Chemistry, 16, 10380-10396.  
20052994 M.A.Smith, P.Pirrat, A.R.Pearson, C.R.Kurtis, C.H.Trinh, T.G.Gaule, P.F.Knowles, S.E.Phillips, and M.J.McPherson (2010).
Exploring the roles of the metal ions in Escherichia coli copper amine oxidase.
  Biochemistry, 49, 1268-1280.
PDB codes: 2wo0 2wof 2woh
19585034 J.Echeverría, E.Cremades, A.J.Amoroso, and S.Alvarez (2009).
Jahn-Teller distortions of six-coordinate CuII compounds: cis or trans?
  Chem Commun (Camb), 0, 4242-4244.  
  18607080 D.B.Langley, D.M.Trambaiolo, A.P.Duff, D.M.Dooley, H.C.Freeman, and J.M.Guss (2008).
Complexes of the copper-containing amine oxidase from Arthrobacter globiformis with the inhibitors benzylhydrazine and tranylcypromine.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 577-583.
PDB codes: 1w4n 1w5z
18838796 H.Ota, H.Tamezane, Y.Sasano, E.Hokazono, Y.Yasuda, S.Sakasegawa, S.Imamura, T.Tamura, and S.Osawa (2008).
Enzymatic characterization of an amine oxidase from Arthrobacter sp. used to measure phosphatidylethanolamine.
  Biosci Biotechnol Biochem, 72, 2732-2738.  
18771294 M.S.Rogers, R.Hurtado-Guerrero, S.J.Firbank, M.A.Halcrow, D.M.Dooley, S.E.Phillips, P.F.Knowles, and M.J.McPherson (2008).
Cross-link formation of the cysteine 228-tyrosine 272 catalytic cofactor of galactose oxidase does not require dioxygen.
  Biochemistry, 47, 10428-10439.
PDB codes: 2vz1 2vz3
  19052360 P.Pirrat, M.A.Smith, A.R.Pearson, M.J.McPherson, and S.E.Phillips (2008).
Structure of a xenon derivative of Escherichia coli copper amine oxidase: confirmation of the proposed oxygen-entry pathway.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 1105-1109.
PDB code: 2w0q
18998639 S.Ghosh, J.Cirera, M.A.Vance, T.Ono, K.Fujisawa, and E.I.Solomon (2008).
Spectroscopic and electronic structure studies of phenolate Cu(II) complexes: phenolate ring orientation and activation related to cofactor biogenesis.
  J Am Chem Soc, 130, 16262-16273.  
17409383 B.J.Johnson, J.Cohen, R.W.Welford, A.R.Pearson, K.Schulten, J.P.Klinman, and C.M.Wilmot (2007).
Exploring molecular oxygen pathways in Hansenula polymorpha copper-containing amine oxidase.
  J Biol Chem, 282, 17767-17776.
PDB codes: 2oov 2oqe
18003930 M.Y.Pau, J.D.Lipscomb, and E.I.Solomon (2007).
Substrate activation for O2 reactions by oxidized metal centers in biology.
  Proc Natl Acad Sci U S A, 104, 18355-18362.  
  17077478 D.B.Langley, A.P.Duff, H.C.Freeman, and J.M.Guss (2006).
The copper-containing amine oxidase from Arthrobacter globiformis: refinement at 1.55 and 2.20 A resolution in two crystal forms.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 1052-1057.
PDB codes: 1w6c 1w6g
15976297 L.M.Mirica, M.Vance, D.J.Rudd, B.Hedman, K.O.Hodgson, E.I.Solomon, and T.D.Stack (2005).
Tyrosinase reactivity in a model complex: an alternative hydroxylation mechanism.
  Science, 308, 1890-1892.  
15148379 O.T.Magnusson, H.Toyama, M.Saeki, A.Rojas, J.C.Reed, R.C.Liddington, J.P.Klinman, and R.Schwarzenbacher (2004).
Quinone biogenesis: Structure and mechanism of PqqC, the final catalyst in the production of pyrroloquinoline quinone.
  Proc Natl Acad Sci U S A, 101, 7913-7918.
PDB codes: 1otv 1otw
14690425 A.P.Duff, A.E.Cohen, P.J.Ellis, J.A.Kuchar, D.B.Langley, E.M.Shepard, D.M.Dooley, H.C.Freeman, and J.M.Guss (2003).
The crystal structure of Pichia pastoris lysyl oxidase.
  Biochemistry, 42, 15148-15157.
PDB code: 1n9e
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.