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J. Biol. Chem., Vol. 275, Issue 50, 39339-39344, December 15, 2000
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From the Hemocyanins are large oligomeric respiratory
proteins found in many arthropods and molluscs. The hemocyanin of the
tarantula Eurypelma californicum is a 24-mer protein
complex with molecular mass of 1,726,459 Da that consists of
seven different polypeptides (a-g), each occupying a
distinct position within the native molecule. Here we report the
complete molecular structure of the E. californicum hemocyanin as deduced from the corresponding cDNAs. This represents the first complex arthropod hemocyanin to be completely sequenced. The
different subunits display 52-66% amino acid sequence identity. Within the subunits, the central domain, which bears the active center
with the copper-binding sites A and B, displays the highest degree of
identity. Using a homology modeling approach, the putative three-dimensional structure of individual subunits was deduced and
compared. Phylogenetic analyses suggest that differentiation of the
individual subunits occurred 400-550 million years ago. The hemocyanin
of the stemline Chelicerata was probably a hexamer built up of six
distinct subunit types a, b/c, d,
e, f, and g, whereas that of the
early Arachnida was originally a 24-mer that emerged after the
differentiation of subunits b and c.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ290429, AJ277489, AJ290430, AJ277491, and AJ277492.
Complete Sequence of the 24-mer Hemocyanin of the Tarantula
Eurypelma californicum
STRUCTURE AND INTRAMOLECULAR EVOLUTION OF THE SUBUNITS*
§,
,
, and
Division of Molecular Biology of the Cell
II, German Cancer Research Center, Im Neuenheimer Feld 280, D-69120
Heidelberg, Germany, the ¶ Institute of Zoology, University of
Munich, Luisenstrasse 14, D-80333 München, Germany, the
Institute of Biophysics, University of Mainz, Welderweg 26, D-55099 Mainz, Germany, and the ** Institute of Zoology, University
of Mainz, Müllerweg 6, D-55099 Mainz, Germany
*
This work has been supported by Deutsche
Forschungsgemeinschaft Grant Bu956/3.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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