2J5W

Ceruloplasmin revisited: structural and functional roles of various metal cation binding sites

2J5W の概要

• エントリーDOI: 10.2210/pdb2j5w/pdb
• 関連するPDBエントリー: 1KCW
• 分子名称: CERULOPLASMIN, CALCIUM ION, SODIUM ION, ... (9 entities in total)
• 機能のキーワード: oxidoreductase, plasma protein, copper transport, copper, transport, polymorphism, glycoprotein, multi-copper oxidase, ceruloplasmin, metal-binding, ion transport
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 123569.42

構造登録者

Bento, I.,Peixoto, C.,Zaitsev, V.N.,Lindley, P.F. (登録日: 2006-09-19, 公開日: 2007-02-06, 最終更新日: 2023-12-13)

主引用文献

Bento, I.,Peixoto, C.,Zaitsev, V.N.,Lindley, P.F.
Ceruloplasmin Revisited: Structural and Functional Roles of Various Metal Cation-Binding Sites.
Acta Crystallogr.,Sect.D, 63:240-, 2007

PubMed Abstract: The three-dimensional molecular structure of human serum ceruloplasmin has been reinvestigated using X-ray synchrotron data collected at 100 K from a crystal frozen to liquid-nitrogen temperature. The resulting model, with an increase in resolution from 3.1 to 2.8 A, gives an overall improvement of the molecular structure, in particular the side chains. In addition, it enables the clear definition of previously unidentified Ca2+-binding and Na+-binding sites. The Ca2+ cation is located in domain 1 in a configuration very similar to that found in the activated bovine factor Va. The Na+ sites appear to play a structural role in providing rigidity to the three protuberances on the top surface of the molecule. These features probably help to steer substrates towards the mononuclear copper sites prior to their oxidation and to restrict the size of the approaching substrate. The trinuclear copper centre appears to differ from the room-temperature structure in that a dioxygen moiety is bound in a similar way to that found in the endospore coat protein CotA from Bacillus subtilis.

PubMed: 17242517
DOI: 10.1107/S090744490604947X

実験手法

X-RAY DIFFRACTION (2.8 Å)