S
IPR028871

Blue (type 1) copper protein, binding site

InterPro entry
Short nameBlueCu_1_BS

Description

Blue (type 1) copper proteins constitute a diverse class of proteins, including small blue proteins and multicopper oxidases. They bind copper and are characterised by an intense electronic absorption band near 600 nm
[2, 1]
.

The most well known members of this class of proteins are the small blue proteins, which includes azurins and plastocyanins. It is a group of monomeric proteins which contain one copper ion per molecule. The plant chloroplastic plastocyanins exchange electrons with cytochrome c6, and the distantly related bacterial azurins exchange electrons with cytochrome c551. This group also includes amicyanin from bacteria such as Methylobacterium extorquens or Paracoccus versutus (Thiobacillus versutus) that can grow on methylamine; auracyanins A and B from Chloroflexus aurantiacus
[6]
; blue copper protein from Alcaligenes faecalis; cupredoxin (CPC) from Cucumis sativus (Cucumber) peelings
[4]
; cusacyanin (basic blue protein; plantacyanin, CBP) from cucumber; halocyanin from Natronomonas pharaonis (Natronobacterium pharaonis)
[3]
, a membrane associated copper-binding protein; pseudoazurin from Pseudomonas; rusticyanin from Thiobacillus ferrooxidans
[5]
; stellacyanin from Rhus vernicifera (Japanese lacquer tree); umecyanin from the roots of Armoracia rusticana (Horseradish); and allergen Ra3 from ragweed. This pollen protein is evolutionary related to the above proteins, but seems to have lost the ability to bind copper.

Although there is an appreciable amount of divergence in the sequences of all these proteins, the copper ligand sites are conserved. This entry represents a conserved site that includes two of the ligands: a cysteine and a histidine.

References

1.Evolution of protein complexity: the blue copper-containing oxidases and related proteins. Ryden LG, Hunt LT. J. Mol. Evol. 36, 41-66, (1993). View articlePMID: 8433378

2.The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide. Garrett TP, Clingeleffer DJ, Guss JM, Rogers SJ, Freeman HC. J. Biol. Chem. 259, 2822-5, (1984). View articlePMID: 6698995

3.The primary structure of halocyanin, an archaeal blue copper protein, predicts a lipid anchor for membrane fixation. Mattar S, Scharf B, Kent SB, Rodewald K, Oesterhelt D, Engelhard M. J. Biol. Chem. 269, 14939-45, (1994). View articlePMID: 8195126

4.The amino acid sequence of a type I copper protein with an unusual serine- and hydroxyproline-rich C-terminal domain isolated from cucumber peelings. Mann K, Schafer W, Thoenes U, Messerschmidt A, Mehrabian Z, Nalbandyan R. FEBS Lett. 314, 220-3, (1992). View articlePMID: 1468551

5.The amino acid sequence of rusticyanin isolated from Thiobacillus ferrooxidans. Yano T, Fukumori Y, Yamanaka T. FEBS Lett. 288, 159-62, (1991). View articlePMID: 1879547

6.Isolation, characterization, and amino acid sequences of auracyanins, blue copper proteins from the green photosynthetic bacterium Chloroflexus aurantiacus. McManus JD, Brune DC, Han J, Sanders-Loehr J, Meyer TE, Cusanovich MA, Tollin G, Blankenship RE. J. Biol. Chem. 267, 6531-40, (1992). View articlePMID: 1313011

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