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8SQO

Crystal Structure of Bacterioferritin (Bfr) from Brucella abortus (magnesium bound, F16L mutant)

8SQO の概要
エントリーDOI10.2210/pdb8sqo/pdb
分子名称Bacterioferritin, MAGNESIUM ION, SULFATE ION, ... (6 entities in total)
機能のキーワードssgcid, structural genomics, seattle structural genomics center for infectious disease, metal binding protein
由来する生物種Brucella abortus 2308
タンパク質・核酸の鎖数1
化学式量合計19819.76
構造登録者
Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2023-05-04, 公開日: 2023-05-17, 最終更新日: 2026-01-14)
主引用文献Liu, L.,Harmon, E.K.,Craig, J.K.,Yao, H.,Battaile, K.P.,Johnson, D.K.,Subramanian, S.,Van Voorhis, W.C.,Rivera, M.,Lovell, S.
Structural Analysis and Inhibitor Modeling of Bacterioferritin From Brucella abortus.
Proteins, 2026
Cited by
PubMed Abstract: Iron homeostasis in various pathogenic bacteria is regulated by bacterioferritins (Bfr) which function to store Fe and release Fe as needed for metabolic processes. The Bfr structure consists of 18 kDa subunits in which dimer pairs bind a heme molecule and are assembled into a highly symmetrical 24-meric spherical structure with an internal core diameter of approximately 80 Å. Release of iron is facilitated by the binding of a 7 kDa [2Fe-2S] ferredoxin (Bfd) to specific sites on the surface of Bfr which transfers electrons to the core thereby reducing the stored Fe to Fe for mobilization. The crystal structures of Bfr from Brucella abortus (Ba) in the apo and iron bound forms are presented and compared with those from Acinetobacter baumannii (Ab) and Pseudomonas aeruginosa (Pa). Additionally, models of the Bfr:Bfd complexes for Ba and Ab are provided and compared with the Pa complex. Finally, compounds known to target the Bfr:Bfd interaction in Pa were docked to the Ba and Ab structures which provided insight regarding the potential binding mode and inhibitory mechanism.
PubMed: 41482512
DOI: 10.1002/prot.70109
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.55 Å)
構造検証レポート
Validation report summary of 8sqo
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2026-04-22に公開中

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