1u9t

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|ACTIVITY=
|ACTIVITY=
|GENE= ChuS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= ChuS ([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=1u9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u9t OCA], [http://www.ebi.ac.uk/pdbsum/1u9t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u9t RCSB]</span>
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[[Category: the montreal-kingston bacterial structural genomics initiative]]
[[Category: the montreal-kingston bacterial structural genomics initiative]]
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Revision as of 21:07, 30 March 2008


PDB ID 1u9t

Drag the structure with the mouse to rotate
, resolution 2.16Å
Gene: ChuS (Escherichia coli)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

1U9T is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Identification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeats., Suits MD, Pal GP, Nakatsu K, Matte A, Cygler M, Jia Z, Proc Natl Acad Sci U S A. 2005 Nov 22;102(47):16955-60. Epub 2005 Nov 7. PMID:16275907

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