1u9t
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1u9t.gif|left|200px]] | [[Image:1u9t.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1u9t", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | + | {{STRUCTURE_1u9t| PDB=1u9t | SCENE= }} | |
- | + | ||
- | | | + | |
- | }} | + | |
'''Crystal Structure Analysis of ChuS, an E. coli Heme Oxygenase''' | '''Crystal Structure Analysis of ChuS, an E. coli Heme Oxygenase''' | ||
Line 28: | Line 25: | ||
[[Category: Jia, Z.]] | [[Category: Jia, Z.]] | ||
[[Category: Suits, M D.]] | [[Category: Suits, M D.]] | ||
- | [[Category: | + | [[Category: Bsgi]] |
- | [[Category: | + | [[Category: Central beta sheet]] |
- | [[Category: | + | [[Category: Flanked by alpha helice]] |
- | [[Category: | + | [[Category: Structural genomic]] |
- | [[Category: | + | [[Category: Structural repeat]] |
- | [[Category: | + | [[Category: The montreal-kingston bacterial structural genomics initiative]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:56:39 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 07:56, 3 May 2008
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 Page seeded by OCA on Sat May 3 10:56:39 2008