Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli

B.R. Otto, R. Sijbrandi, S. Luirink, B. Oudega, J.G. Heddle, K. Mizutani, S.Y. Park, J.R.H. Tame

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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 β-helical structure yet solved. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
Original languageEnglish
Pages (from-to)17339-17345
Number of pages7
JournalJournal of Biological Chemistry
Volume280
DOIs
Publication statusPublished - 2005

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