3AK5

Hemoglobin protease (Hbp) passenger missing domain-2

Summary for 3AK5

• Entry DOI: 10.2210/pdb3ak5/pdb
• Related: 1WXR 3H09
• Descriptor: Hemoglobin-binding protease hbp, CALCIUM ION (3 entities in total)
• Functional Keywords: autotransporter, beta helix, mutant, hydrolase
• Biological source: Escherichia coli; More
• Cellular location: Hemoglobin-binding protease hbp autotransporter: Periplasm . Hemoglobin-binding protease hbp: Secreted. Hemoglobin-binding protease hbp translocator: Cell outer membrane ; Multi-pass membrane protein : O88093
• Total number of polymer chains: 4
• Total formula weight: 415058.81

Authors

Nishimura, K.,Park, S.-Y.,Tame, J.R.H. (deposition date: 2010-07-07, release date: 2010-10-06, Last modification date: 2023-11-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)