3L6W

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

3L6W の概要

• エントリーDOI: 10.2210/pdb3l6w/pdb
• 関連するPDBエントリー: 3EU2
• 分子名称: Hemocyanin 1 (1 entity in total)
• 機能のキーワード: hemocyanin, cupredoxin domain, copper-binding protein, metal-binding, oxygen binding
• 由来する生物種: Megathura crenulata (Giant keyhole limpet)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 113247.59

構造登録者

Jaenicke, E.,Buechler, K.,Markl, J.,Decker, H.,Barends, T.R.M. (登録日: 2009-12-27, 公開日: 2010-02-02, 最終更新日: 2023-11-01)

主引用文献

Jaenicke, E.,Buchler, K.,Markl, J.,Decker, H.,Barends, T.R.M.
The Cupredoxin-like Domains in Hemocyanins.
Biochem.J., 2009

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: 20025608
DOI: 10.1042/BJ20091501

実験手法

X-RAY DIFFRACTION (4 Å)