4EFQ

Bombyx mori lipoprotein 7 - platinum derivative at 1.94 A resolution

4EFQ の概要

• エントリーDOI: 10.2210/pdb4efq/pdb
• 関連するPDBエントリー: 3PUB 4EFP 4EFR
• 分子名称: 30kDa protein, THIOCYANATE ION, POTASSIUM ION, ... (5 entities in total)
• 機能のキーワード: vhs domain, beta-trefoil, unknown function
• 由来する生物種: Bombyx mori (silk moth,silkworm)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56562.10

構造登録者

Pietrzyk, A.J.,Panjikar, S.,Bujacz, A.,Mueller-Dieckmann, J.,Jaskolski, M.,Bujacz, G. (登録日: 2012-03-30, 公開日: 2012-08-29, 最終更新日: 2024-11-20)

主引用文献

Pietrzyk, A.J.,Panjikar, S.,Bujacz, A.,Mueller-Dieckmann, J.,Lochynska, M.,Jaskolski, M.,Bujacz, G.
High-resolution structure of Bombyx mori lipoprotein 7: crystallographic determination of the identity of the protein and its potential role in detoxification.
Acta Crystallogr.,Sect.D, 68:1140-1151, 2012

PubMed Abstract: Three crystal structures of a lipoprotein (Bmlp7) of unknown function, a member of the 30 kDa lipoprotein family from mulberry silkworm (Bombyx mori L.) haemolymph, have been determined. The 1.33 Å resolution structure is an excellent example of how a precise crystallographic study can contribute to protein identification. The correct sequence of this haemolymph-isolated protein was assigned thanks to superb-quality electron-density maps. Two unexpected cadmium cations were found in this crystal structure [Bmlp7-I(Cd)] and their presence may be connected to a detoxification mechanism in this insect. For a comparison of the metal-binding sites, the crystal structure of a platinum complex (Bmlp7-Pt) was also solved at 1.94 Å resolution. The third (2.50 Å resolution) structure, of the native protein harvested in a different season (Bmlp7-II), corresponds to a different polymorph with an altered pattern of intermolecular interactions and with a total absence of cadmium ions and highlights the possible involvement of Bmlp7 in the response to environmental pollution. The N-terminal domain of Bmlp7 has a fold resembling a clockwise spiral created by six helices and can be classified as a VHS domain. The C-terminal domain is folded as a β-trefoil. The biological function of Bmlp7 is unknown, but its structural homology to sugar-binding proteins suggests that, in analogy to other 30 kDa haemolymph lipoproteins, it could play a role as an anti-apoptotic factor or function in the immune response of the insect to fungal infections.

PubMed: 22948915
DOI: 10.1107/S0907444912021555

実験手法

X-RAY DIFFRACTION (1.94 Å)