1U9T

Crystal Structure Analysis of ChuS, an E. coli Heme Oxygenase

Summary for 1U9T

• Entry DOI: 10.2210/pdb1u9t/pdb
• Descriptor: putative heme/hemoglobin transport protein (2 entities in total)
• Functional Keywords: structural genomics, the montreal-kingston bacterial structural genomics initiative, structural repeat, central beta sheet, flanked by alpha helices, bsgi, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 40052.02

Authors

Suits, M.D.,Jia, Z.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2004-08-10, release date: 2005-10-25, Last modification date: 2024-02-14)

Primary citation

Suits, M.D.,Pal, G.P.,Nakatsu, K.,Matte, A.,Cygler, M.,Jia, Z.
Identification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeats
Proc.Natl.Acad.Sci.Usa, 102:16955-16960, 2005

PubMed Abstract: Heme oxygenases (HOs) catalyze the oxidation of heme to biliverdin, carbon monoxide (CO), and free iron. Iron acquisition is critical for invading microorganisms to enable survival and growth. Here we report the crystal structure of ChuS, which displays a previously uncharacterized fold and is unique compared with other characterized HOs. Despite only 19% sequence identity between the N- and C-terminal halves, these segments of ChuS represent a structural duplication, with a root-mean-square deviation of 2.1 A between the two repeats. ChuS is capable of using ascorbic acid or cytochrome P450 reductase-NADPH as electron sources for heme oxygenation. CO detection confirmed that ChuS is a HO, and we have identified it in pathogenic Escherichia coli O157:H7. Based on sequence analysis, this HO is present in many bacteria, although not in the E. coli K-12 strain. The N- and C-terminal halves of ChuS are each a functional HO.

PubMed: 16275907
DOI: 10.1073/pnas.0504289102

Experimental method

X-RAY DIFFRACTION (2.16 Å)