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Conformational stabilization at the active site of molluskan (Rapana thomasiana) hemocyanin by a cysteine-histidine thioether bridge - A study by mass spectrometry and molecular modeling
Gielens, C.; Idakieva, K.; De Maeyer, M.; Van den Bergh, V.; Siddiqui, N.I.; Compernolle, F. (2007). Conformational stabilization at the active site of molluskan (Rapana thomasiana) hemocyanin by a cysteine-histidine thioether bridge - A study by mass spectrometry and molecular modeling. Peptides (New York, NY : 1980) 28(4): 790-797. https://dx.doi.org/10.1016/j.peptides.2006.12.004
In: Peptides. Elsevier: New York etc.. ISSN 0196-9781; e-ISSN 1873-5169, meer
Peer reviewed article  
Beschikbaar in  Auteurs 
Trefwoorden
    Rapana thomasiana Crosse, 1861 [WoRMS]
    Marien/Kust
Author keywords
    copper type-3 proteins; cysteine-histidine thioether bridge; dead-endelimination; electrospray ionization mass spectrometry; hemocyanin;Rapana thomasiana
Auteurs  Top 
  • Gielens, C., meer
  • Idakieva, K.
  • De Maeyer, M.
  • Van den Bergh, V.
  • Siddiqui, N.I.
  • Compernolle, F.
Abstract
    In some type-3 copper proteins (molluskan hemocyanin, catechol oxidase and fungal tyrosinase) one of the histidine residues, liganding the CuA atom of the dinuclear copper active site, is covalently linked to a cysteine residue by a thioether bridge. The purpose of this study was to disclose the function of this bridge. Mass spectral analysis of a peptide, isolated from Rapana thomasiana (gastropodan mollusk) hemocyanin, indicated a stabilization of the peptide structure in the region of the bridge. Molecular modeling of three thioether containing type-3 copper proteins using the dead-end elimination method showed that the concerned histidine would be very flexible if not linked to the cysteine. Also, the side chain orientation of the histidine is rather exceptional, as evidenced by statistical data from the protein databank. It is suggested that the role of the bridge is to fix the histidine in an orientation that is optimal for coordination of the CuA atom.
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