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Journal Article

Cupredoxin-like domains in haemocyanins

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Barends,  Thomas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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http://www.biochemj.org/content/426/3/373.full-text.pdf
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https://dx.doi.org/10.1042/BJ20091501
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Citation

Jaenicke, E., Büchler, K., Markl, J., Decker, H., & Barends, T. (2010). Cupredoxin-like domains in haemocyanins. Biochemical Journal, 426(3), 373-378. doi:10.1042/BJ20091501.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002C-5720-1
Abstract
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 but 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.