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PDBsum entry 1id2
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protein metals Protein-protein interface(s) links
Electron transport PDB id
1id2

 

 

 

 

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Contents
Protein chains
106 a.a. *
Metals
_CU ×3
Waters ×122
* Residue conservation analysis
PDB id:
1id2
Name: Electron transport
Title: Crystal structure of amicyanin from paracoccus versutus (thiobacillus versutus)
Structure: Amicyanin. Chain: a, b, c. Engineered: yes
Source: Paracoccus versutus. Organism_taxid: 34007. Gene: mauc or ami. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.15Å     R-factor:   0.174    
Authors: A.Romero,H.Nar,A.Messerschmidt
Key ref:
A.Romero et al. (1994). Crystal structure analysis and refinement at 2.15 A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus. J Mol Biol, 236, 1196-1211. PubMed id: 8120896 DOI: 10.1016/0022-2836(94)90021-3
Date:
03-Apr-01     Release date:   11-Apr-01    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P22365  (AMCY_PARVE) -  Amicyanin from Paracoccus versutus
Seq:
Struc: 		132 a.a.
106 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/0022-2836(94)90021-3 J Mol Biol 236:1196-1211 (1994)
PubMed id: 8120896  
 
 
Crystal structure analysis and refinement at 2.15 A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus.
A.Romero, H.Nar, R.Huber, A.Messerschmidt, A.P.Kalverda, G.W.Canters, R.Durley, F.S.Mathews.
 
  ABSTRACT  
 
The crystal structure of the type I blue copper protein amicyanin from Thiobacillus versutus has been determined by Patterson search techniques on the basis of the molecular model of amicyanin from Paracoccus denitrificans, and refined by energy-restrained least-squares methods. Amicyanin crystallizes in the trigonal space group P3(2) with unit cell dimensions of a = b = 87.40 A, c = 38.20 A. The asymmetric unit is composed of three independent molecules centred on the crystallographic 3(2) axes. The final R-value is 17.4% for 15,984 reflections to a resolution of 2.15 A. The polypeptide fold in amicyanin is based on the beta-sandwich structure commonly found in blue copper proteins. Nine beta strands are folded into two twisted beta-sheets that pack together with a filling of non-polar residues between them. The geometry of the copper site is similar to that of plastocyanin. There are four ligands, arranged approximately as a distorted tetrahedron, to the copper atom: His54, Cys93, His96 and Met99. One of the copper ligands, His96, is exposed to the surface and lies in the centre of a cluster of seven hydrophobic residues.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. A section (z= 14/42) of the difference Patterson map compute at 3.5 A resolution. Two sites relaed by translation of z, ) = (2/3, l/3) g' Ives rse to identical position in the difference Patterson map which in turn explains the elative peak heights of 2 : I or the 2 Harker peaks. 		Figure 8.
Fgure 8. C:rvstal acking of amicyanin from T. versrt&. The 3 independent molecules of amicyanin are arranged as
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1994, 236, 1196-1211) copyright 1994.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18250895 C.Dennison (2008).
The role of ligand-containing loops at copper sites in proteins.
  Nat Prod Rep, 25, 15-24.  
16795108 K.Sato, and C.Dennison (2006).
Active site comparison of CoII blue and green nitrite reductases.
  Chemistry, 12, 6647-6659.  
16234922 C.Dennison (2005).
Ligand and loop variations at type 1 copper sites: influence on structure and reactivity.
  Dalton Trans, (), 3436-3442.  
15048833 M.D.Harrison, and C.Dennison (2004).
Characterization of Arabidopsis thaliana stellacyanin: a comparison with umecyanin.
  Proteins, 55, 426-435.  
12885256 G.Battistuzzi, M.Bellei, M.Borsari, G.W.Canters, E.de Waal, L.J.Jeuken, A.Ranieri, and M.Sola (2003).
Control of metalloprotein reduction potential: compensation phenomena in the reduction thermodynamics of blue copper proteins.
  Biochemistry, 42, 9214-9220.  
12794870 V.Cunsolo, S.Foti, C.La Rosa, R.Saletti, G.W.Canters, and M.P.Verbeet (2003).
Monitoring of unfolding of metallo-proteins by electrospray ionization mass spectrometry.
  J Mass Spectrom, 38, 502-509.  
12450394 G.Battistuzzi, M.Borsari, G.W.Canters, E.de Waal, A.Leonardi, A.Ranieri, and M.Sola (2002).
Thermodynamics of the acid transition in blue copper proteins.
  Biochemistry, 41, 14293-14298.  
11565099 V.Cunsolo, S.Foti, C.La Rosa, R.Saletti, G.W.Canters, and M.P.Verbeet (2001).
Free energy for blue copper protein unfolding determined by electrospray ionisation mass spectrometry.
  Rapid Commun Mass Spectrom, 15, 1817-1825.  
10818346 K.C.Cheung, R.W.Strange, and S.S.Hasnain (2000).
3D EXAFS refinement of the Cu site of azurin sheds light on the nature of structural change at the metal centre in an oxidation-reduction process: an integrated approach combining EXAFS and crystallography.
  Acta Crystallogr D Biol Crystallogr, 56, 697-704.  
10924152 R.E.Diederix, G.W.Canters, and C.Dennison (2000).
The Met99Gln mutant of amicyanin from Paracoccus versutus.
  Biochemistry, 39, 9551-9560.  
9188741 A.V.Efimov (1997).
Structural trees for protein superfamilies.
  Proteins, 28, 241-260.  
8589245 R.Fattorusso, G.Morelli, A.Lombardi, F.Nastri, O.Maglio, G.D'Auria, C.Pedone, and V.Pavone (1995).
Design of metal ion binding peptides.
  Biopolymers, 37, 401-410.  
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.

 

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