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1I4H

Crystal structure of Zn2+ soaked Staphylococcal enterotoxin A mutant H187A

1I4H の概要
エントリーDOI10.2210/pdb1i4h/pdb
関連するPDBエントリー1EFS 1I4G 1SXT
分子名称ENTEROTOXIN TYPE A, ZINC ION (2 entities in total)
機能のキーワードbeta-grasp, beta-barrel, toxin
由来する生物種Staphylococcus aureus
細胞内の位置Secreted: P0A0L2
タンパク質・核酸の鎖数2
化学式量合計54257.29
構造登録者
Hakansson, M.,Antonsson, P.,Bjork, P.,Svensson, L.A. (登録日: 2001-02-21, 公開日: 2001-02-28, 最終更新日: 2024-11-06)
主引用文献Hakansson, M.,Antonsson, P.,Bjork, P.,Svensson, L.A.
Cooperative zinc binding in a staphylococcal enterotoxin A mutant mimics the SEA-MHC class II interaction
J.Biol.Inorg.Chem., 6:757-762, 2001
Cited by
PubMed Abstract: The structure of a mutant form of staphylococcal enterotoxin A (SEA) has been determined to 2.1 A resolution. The studied SEA substitution H187-->A187 (SEAH187A) leads to an almost 10-fold reduction of the binding to major histocompatibility complex (MHC) class II. H187 is important for this interaction since it coordinates Zn2+. The zinc ion is thought to hold MHC class II and SEA together in a complex. Interestingly, only one of two molecules in the asymmetric unit binds Zn2+. H225, D227, a water molecule, and H44 from a symmetry-related molecule ligate Zn2+. The symmetry-related histidine is necessary for this substituted Zn2+ site to bind to Zn2+ at low zinc concentration (no Zn2+ added). Since a water molecule replaces the missing H187, H44 binds Zn2+ at the position where betaH81 from MHC class II probably will bind. Dynamic light scattering analysis reveals that in solution as well as in the crystal lattice the SEA(H187A) mutant forms aggregates. The substitution per se does not cause aggregation since wild-type SEA also forms aggregates. Addition of EDTA reduces the size of the aggregates, indicating a cross-linking function of Zn2+. In agreement with the biological function, the aggregation is weak (i.e. not revealed by gel filtration) and non-specific.
PubMed: 11713682
DOI: 10.1007/s007750100251
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.9 Å)
構造検証レポート
Validation report summary of 1i4h
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-04-02に公開中

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