3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin

Autor:	Nell M. Soeter, Henk J. Bak, J.J. Beintema, Johan M. Vereijken, W. P. J. Gaykema, Wim G. J. Hol
Rok vydání:	1984
Předmět:	Crystallography Multidisciplinary Oxygen-carrying chemistry Panulirus Protein subunit chemistry.chemical_element Random hexamer Biology biology.organism_classification Peptide sequence Copper
Zdroj:	Nature. 309:23-29
ISSN:	1476-4687 0028-0836
DOI:	10.1038/309023a0
Popis:	For the first time, the three-dimensional structure of a member of the copper-containing class of oxygen-carrying proteins—the haemocyanins—has been determined. The structure of Panulirus interruptus haemocyanin at 3.2 A resolution shows that each subunit of the 450,000-molecular weight hexamer is folded into three domains, and that the binuclear copper site is situated in the centre of the second domain. Amino acid sequence comparisons suggest that the polypeptide fold of P. interruptus haemocyanin is common to all arthropod haemocyanins.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::34ad25d0cef5753f55e6273629c678a4 https://doi.org/10.1038/309023a0 Zobrazit plný text záznamu