3AK5

Hemoglobin protease (Hbp) passenger missing domain-2

3AK5 の概要

• エントリーDOI: 10.2210/pdb3ak5/pdb
• 関連するPDBエントリー: 1WXR 3H09
• 分子名称: Hemoglobin-binding protease hbp, CALCIUM ION (3 entities in total)
• 機能のキーワード: autotransporter, beta helix, mutant, hydrolase
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Hemoglobin-binding protease hbp autotransporter: Periplasm . Hemoglobin-binding protease hbp: Secreted. Hemoglobin-binding protease hbp translocator: Cell outer membrane ; Multi-pass membrane protein : O88093
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 415058.81

構造登録者

Nishimura, K.,Park, S.-Y.,Tame, J.R.H. (登録日: 2010-07-07, 公開日: 2010-10-06, 最終更新日: 2023-11-01)

主引用文献

Nishimura, K.,Yoon, Y.-H.,Kurihara, A.,Unzai, S.,Luirink, J.,Park, S.-Y.,Tame, J.R.H.
Role of domains within the autotransporter Hbp/Tsh
Acta Crystallogr.,Sect.D, 66:1295-1300, 2010

PubMed Abstract: The autotransporter Tsh (temperature-sensitive haemagglutinin) secreted by avian pathogenic Escherichia coli was reported in 1994 and the almost identical Hbp (haemoglobin protease) was discovered some years later in isolates from patients suffering from peritoneal abscesses. However, the function of the protein remains uncertain. The crystal structure of Hbp shows that the protein carries a serine protease domain (domain 1) and a small domain of 75 residues called domain 2 which is inserted into the long β-helix characteristic of autotransporter passenger proteins. In this paper, domain 1 is shown to bind calcium, although metal ions binding to this site do not seem to regulate protease activity. Tsh has been reported to bind red cells and components of the extracellular matrix, but it is demonstrated that these properties are not a consequence of the presence of domain 2.

PubMed: 21123869
DOI: 10.1107/S0907444910036966

実験手法

X-RAY DIFFRACTION (2.2 Å)