Structure of arthropod hemocyanin

FEBS Letters

Bak, Henk J.¹  Jekel, Peter A.¹  Soeter, Nell M.¹  Neuteboom, Ben¹  Vereijken, Johan M.¹  Beintema, Jaap J.¹ 

[1] Biochemisch Laboratorium, Rijksuniversiteit Groningen, Nijenborgh 16; 9747 AG Groningen, The Netherlands

关键词: (Panulirus interruptus);    Hemocyanin;    Amino acid sequence;    Molecular evolution;   

DOI  :  10.1016/0014-5793(86)81402-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown