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

Research output: Contribution to JournalArticleAcademicpeer-review

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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Escherichia coli Proteins
Heme
Hemoglobins
Peptide Hydrolases
Crystal structure
Escherichia coli
Serine Proteases
Iron
Abdominal Abscess
Bacteroides fragilis
Symbiosis
Bacteria
Carrier Proteins
Type V Secretion Systems
heme-binding protein
Proteins

Cite this

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title = "Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli",
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. {\circledC} 2005 by The American Society for Biochemistry and Molecular Biology, Inc.",
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Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli. / Otto, B.R.; Sijbrandi, R.; Luirink, S.; Oudega, B.; Heddle, J.G.; Mizutani, K.; Park, S.Y.; Tame, J.R.H.

In: Journal of Biological Chemistry, Vol. 280, 2005, p. 17339-17345.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli

AU - Otto, B.R.

AU - Sijbrandi, R.

AU - Luirink, S.

AU - Oudega, B.

AU - Heddle, J.G.

AU - Mizutani, K.

AU - Park, S.Y.

AU - Tame, J.R.H.

PY - 2005

Y1 - 2005

N2 - 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.

AB - 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.

U2 - 10.1074/jbc.M412885200

DO - 10.1074/jbc.M412885200

M3 - Article

VL - 280

SP - 17339

EP - 17345

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

ER -