1WXR

Crystal structure of Heme Binding protein, an autotransporter hemoglobine protease from pathogenic Escherichia coli

Summary for 1WXR

• Entry DOI: 10.2210/pdb1wxr/pdb
• Descriptor: haemoglobin protease (2 entities in total)
• Functional Keywords: hemoglobine protease, autotransporter, beta helix, heme uptake, spate, hydrolase
• Biological source: Escherichia coli
• Cellular location: Hemoglobin-binding protease hbp autotransporter: Periplasm (By similarity). Hemoglobin-binding protease hbp: Secreted. Hemoglobin-binding protease hbp translocator: Cell outer membrane; Multi-pass membrane protein (By similarity): O88093
• Total number of polymer chains: 1
• Total formula weight: 111963.58

Authors

Otto, B.R.,Sijbrandi, R.,Luirink, J.,Oudega, B.,Heddle, J.G.,Mizutani, K.,Park, S.-Y.,Tame, J.R.H. (deposition date: 2005-01-31, release date: 2005-03-01, Last modification date: 2024-03-13)

Primary citation

Otto, B.R.,Sijbrandi, R.,Luirink, J.,Oudega, B.,Heddle, J.G.,Mizutani, K.,Park, S.-Y.,Tame, J.R.H.
Crystal structure of heme binding protein, an autotransporter hemoglobin protease from pathogenic escherichia coli
J.Biol.Chem., 280:17339-17345, 2005

PubMed Abstract: The acquisition of iron is essential for the survival of pathogenic bacteria, which have consequently evolved a wide variety of uptake systems to extract iron and heme from host proteins such as hemoglobin. Hemoglobin protease (Hbp) was discovered as a factor involved in the symbiosis of pathogenic Escherichia coli and Bacteroides fragilis, which cause intra-abdominal abscesses. Released from E. coli, this serine protease autotransporter degrades hemoglobin and delivers heme to both bacterial species. The crystal structure of the complete passenger domain of Hbp (110 kDa) is presented, which is the first structure from this class of serine proteases and the largest parallel beta-helical structure yet solved.

PubMed: 15728184
DOI: 10.1074/jbc.M412885200

Experimental method

X-RAY DIFFRACTION (2.2 Å)