期刊
BIOCHEMICAL JOURNAL
卷 426, 期 -, 页码 373-378出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20091501
关键词
copper protein; cupredoxin; evolution; haemocyanin (hemocyanin); keyhole-limpet-haemocyanin (KLH); Mollusca
资金
- International Graduate School of Immunotherapy [Deutsche Forschungschaft] [GK 1043]
- Immunology Research Center of the Johannes Gutenberg University, Mainz, Germany
Haemocyanins are multimeric oxygen transport proteins, which bind oxygen to type 3 copper sites, Arthropod haemocyanins contain 75-kDa subunits, whereas molluscan haemocyanins contain 350-400-kDa Subunits comprising seven or eight different 50 kDa FUs (functional units) designated FU-a to FU-h each with an active site. FU-h possesses a tail of 100 amino acids not present in the other FUs. In the present study we show by X-ray crystallography that in FU-h of KLH1 (keyhole-limpet-haemocyanin isoform 1) the structure of the tail domain is cupredoxin-like bill contains no copper. The copper-free domain 3 in arthropod haemocyanin subunits has also recently been reinterpreted as being cupredoxin-like. We propose that the cupredoxin-like domain in both haemocyanin types once served to upload copper to the active site of the oxygen-binding domain.
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