3l6w

Structure of the collar functional unit (KLH1-H) of keyhole limpet hemocyanin

spinqualitylabelsall models 3l6w, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3l6w is a 2 chain structure with sequence from Megathura crenulata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HCY1_MEGCR Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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