1wxr

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|ACTIVITY=
|ACTIVITY=
|GENE= HBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= HBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wxr OCA], [http://www.ebi.ac.uk/pdbsum/1wxr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wxr RCSB]</span>
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[[Category: spate]]
[[Category: spate]]
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Revision as of 21:42, 30 March 2008


PDB ID 1wxr

Drag the structure with the mouse to rotate
, resolution 2.20Å
Gene: HBP (Escherichia coli)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

1WXR is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli., Otto BR, Sijbrandi R, Luirink J, Oudega B, Heddle JG, Mizutani K, Park SY, Tame JR, J Biol Chem. 2005 Apr 29;280(17):17339-45. Epub 2005 Feb 22. PMID:15728184

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