Structure of arthropod hemocyanin

Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. The amino acid sequence of subunit a of Panulirus interruptus hemocyanin (657 residues) has been completed and fitted to the electron-density map (3.2 Å resolution). Comparison of amino acid se...

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Bibliographic Details
Published in:FEBS letters 1986-08, Vol.204 (1), p.141-144
Main Authors: Bak, Henk J., Neuteboom, Ben, Jekel, Peter A., Soeter, Nell M., Vereijken, Johan M., Beintema, Jaap J.
Format: Article
Language:English
Subjects:
Amino acid sequence
amino acids
Analytical, structural and metabolic biochemistry
Biological and medical sciences
evolution
Fundamental and applied biological sciences. Psychology
Hemocyanin
hemocyanins
Marine
Metalloproteins
Molecular evolution
molecular structure
Other metalloproteins
Panulirus interruptus
Proteins
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Summary:Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. The amino acid sequence of subunit a of Panulirus interruptus hemocyanin (657 residues) has been completed and fitted to the electron-density map (3.2 Å resolution). Comparison of amino acid sequence data for several different hemocyanin subunits of arthropod species indicated that the general features of the polypeptide architecture as found in spiny lobster hemocyanin occur in all arthropods. This structure must therefore be at least as old as the estimated time of divergence of crustaceans and chelicerates, 540–600 million years ago.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(86)81402-8