Structural highlights
Function
HCY1_MEGCR Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Cupredoxin-like domains in haemocyanins.,Jaenicke E, Buchler K, Markl J, Decker H, Barends TR Biochem J. 2010 Feb 24;426(3):373-8. PMID:20025608[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Swerdlow RD, Ebert RF, Lee P, Bonaventura C, Miller KI. Keyhole limpet hemocyanin: structural and functional characterization of two different subunits and multimers. Comp Biochem Physiol B Biochem Mol Biol. 1996 Mar;113(3):537-48. PMID:8829804 doi:10.1016/0305-0491(95)02091-8
- ↑ Jaenicke E, Buchler K, Markl J, Decker H, Barends TR. Cupredoxin-like domains in haemocyanins. Biochem J. 2010 Feb 24;426(3):373-8. PMID:20025608 doi:10.1042/BJ20091501
