3ak5 | pdb_00003ak5
Hemoglobin protease (Hbp) passenger missing domain-2
Structural highlights
FunctionHBP_ECOLX Interacts with hemoglobin, degrades it and subsequently binds the released heme. Could make heme accessible not only for E.coli, but also for B.fragilis during mixed intra-abdominal infections. Has a role in abscess formation.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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 beta-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. Role of domains within the autotransporter Hbp/Tsh.,Nishimura K, Yoon YH, Kurihara A, Unzai S, Luirink J, Park SY, Tame JR Acta Crystallogr D Biol Crystallogr. 2010 Dec;66(Pt 12):1295-300. Epub, 2010 Nov 16. PMID:21123869[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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