1u9t
From Proteopedia
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- | [[Image:1u9t.gif|left|200px]] | + | [[Image:1u9t.gif|left|200px]] |
- | + | ||
- | '''Crystal Structure Analysis of ChuS, an E. coli Heme Oxygenase''' | + | {{Structure |
+ | |PDB= 1u9t |SIZE=350|CAPTION= <scene name='initialview01'>1u9t</scene>, resolution 2.16Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= ChuS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure Analysis of ChuS, an E. coli Heme Oxygenase''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1U9T is a [ | + | 1U9T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U9T OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16275907 16275907] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: bsgi]] | [[Category: bsgi]] | ||
[[Category: central beta sheet]] | [[Category: central beta sheet]] | ||
- | [[Category: flanked by alpha | + | [[Category: flanked by alpha helice]] |
- | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: structural repeat]] | [[Category: structural repeat]] | ||
[[Category: the montreal-kingston bacterial structural genomics initiative]] | [[Category: the montreal-kingston bacterial structural genomics initiative]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:29:12 2008'' |
Revision as of 12:29, 20 March 2008
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, resolution 2.16Å | |||||||
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Gene: | ChuS (Escherichia coli) | ||||||
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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