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PDBsum entry 3fpy

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protein ligands metals links
Electron transport PDB id
3fpy

 

 

 

 

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Contents
Protein chain
128 a.a. *
Ligands
TRS
Metals
_CU ×2
Waters ×175
* Residue conservation analysis
PDB id:
3fpy
Name: Electron transport
Title: Azurin c112d/m121l
Structure: Azurin. Chain: a. Engineered: yes. Mutation: yes
Source: Pseudomonas aeruginosa. Organism_taxid: 287. Gene: azu, pa4922. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.178     R-free:   0.236
Authors: K.M.Lancaster,H.B.Gray
Key ref: K.M.Lancaster et al. (2009). Type-zero copper proteins. Nat Chem, 1, 711-715. PubMed id: 20305734
Date:
06-Jan-09     Release date:   10-Nov-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00282  (AZUR_PSEAE) -  Azurin from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Seq:
Struc:
148 a.a.
128 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
Nat Chem 1:711-715 (2009)
PubMed id: 20305734  
 
 
Type-zero copper proteins.
K.M.Lancaster, S.DeBeer George, K.Yokoyama, J.H.Richards, H.B.Gray.
 
  ABSTRACT  
 
Copper proteins play key roles in biological processes such as electron transfer and dioxygen activation; the active site of each of these proteins is classified as either type 1, 2, or 3, depending on its optical and electron paramagnetic resonance properties. We have built a new type of site that we call "type zero copper" by incorporating leucine, isoleucine, or phenylalanine in place of methionine at position 121 in C112D Pseudomonas aeruginosa azurin. X-ray crystallographic analysis shows that these sites adopt distorted tetrahedral geometries, with an unusually short Cu-O(G45 carbonyl) bond (2.35-2.55 A). Relatively weak absorption near 800 nm and narrow parallel hyperfine splittings in EPR spectra are the spectroscopic signatures of type zero copper. Copper K-edge x-ray absorption spectra suggest elevated Cu(II) 4p character in the d-electron ground state. Cyclic voltammetric experiments demonstrate that the electron transfer reactivities of type zero azurins are enhanced relative to that of the corresponding type 2 (C112D) protein.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21276936 J.Chaboy, S.Díaz-Moreno, I.Díaz-Moreno, M.A.De la Rosa, and A.Díaz-Quintana (2011).
How the local geometry of the Cu-binding site determines the thermal stability of blue copper proteins.
  Chem Biol, 18, 25-31.  
21212876 S.Kume, and H.Nishihara (2011).
Synchronized motion and electron transfer of a redox-active rotor.
  Dalton Trans, 40, 2299-2305.  
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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