3L6W
Structure of the collar functional unit (KLH1-H) of keyhole limpet hemocyanin
Summary for 3L6W
| Entry DOI | 10.2210/pdb3l6w/pdb |
| Related | 3EU2 |
| Descriptor | Hemocyanin 1 (1 entity in total) |
| Functional Keywords | hemocyanin, cupredoxin domain, copper-binding protein, metal-binding, oxygen binding |
| Biological source | Megathura crenulata (Giant keyhole limpet) |
| Total number of polymer chains | 2 |
| Total formula weight | 113247.59 |
| Authors | Jaenicke, E.,Buechler, K.,Markl, J.,Decker, H.,Barends, T.R.M. (deposition date: 2009-12-27, release date: 2010-02-02, Last modification date: 2023-11-01) |
| Primary citation | Jaenicke, E.,Buchler, K.,Markl, J.,Decker, H.,Barends, T.R.M. The Cupredoxin-like Domains in Hemocyanins. Biochem.J., 2009 Cited by PubMed 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. PubMed: 20025608DOI: 10.1042/BJ20091501 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4 Å) |
Structure validation
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