1wxr
From Proteopedia
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 Page seeded by OCA on Sat May 3 14:16:46 2008
