1QVS

Crystal Structure of Haemophilus influenzae H9A mutant Holo Ferric ion-Binding Protein A

1QVS の概要

• エントリーDOI: 10.2210/pdb1qvs/pdb
• 分子名称: Iron-utilization periplasmic protein, FE (III) ION, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: metal binding protein
• 由来する生物種: Haemophilus influenzae
• 細胞内の位置: Periplasm (Probable): P35755
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34059.66

構造登録者

Shouldice, S.R.,Skene, R.J.,Dougan, D.R.,McRee, D.E.,Tari, L.W.,Schryvers, A.B. (登録日: 2003-08-28, 公開日: 2003-11-04, 最終更新日: 2023-08-16)

主引用文献

Shouldice, S.R.,Skene, R.J.,Dougan, D.R.,McRee, D.E.,Tari, L.W.,Schryvers, A.B.
Presence of ferric hydroxide clusters in mutants of Haemophilus influenzae ferric ion-binding protein A
Biochemistry, 42:11908-11914, 2003

PubMed Abstract: The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. In this study, we report the crystal structures of two mutant forms of ferric ion-binding protein A (FbpA) from Haemophilus influenzae with bound multinuclear oxo-metal clusters. Crystals of site-directed mutants in the metal or anion binding ligands contain protein in the open conformation, and two mutant FbpAs, H9A and N175L, contain different cluster arrangements in the iron-binding pocket. The iron clusters are anchored by binding to the two tyrosine ligands (Tyr195 and Tyr196) positioned at the vertex of the iron-binding pocket but are not coordinated by the other metal binding ligands. Our results suggest that the metal clusters may have formed in situ, suggesting that the mutant FbpAs may serve as a simple model for protein-mediated mineralization.

PubMed: 14556621
DOI: 10.1021/bi035389s

実験手法

X-RAY DIFFRACTION (2.1 Å)