2d40

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[[Image:2d40.gif|left|200px]]<br /><applet load="2d40" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2d40.gif|left|200px]]
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caption="2d40, resolution 2.41&Aring;" />
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'''Crystal Structure of Z3393 from Escherichia coli O157:H7'''<br />
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{{Structure
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|PDB= 2d40 |SIZE=350|CAPTION= <scene name='initialview01'>2d40</scene>, resolution 2.41&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Gentisate_1,2-dioxygenase Gentisate 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.4 1.13.11.4]
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|GENE=
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}}
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'''Crystal Structure of Z3393 from Escherichia coli O157:H7'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2D40 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o127:h6 Escherichia coli o127:h6] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Gentisate_1,2-dioxygenase Gentisate 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.4 1.13.11.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D40 OCA].
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2D40 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o127:h6 Escherichia coli o127:h6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D40 OCA].
==Reference==
==Reference==
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Structural and biochemical characterization of gentisate 1,2-dioxygenase from Escherichia coli O157:H7., Adams MA, Singh VK, Keller BO, Jia Z, Mol Microbiol. 2006 Sep;61(6):1469-84. Epub 2006 Aug 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16930152 16930152]
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Structural and biochemical characterization of gentisate 1,2-dioxygenase from Escherichia coli O157:H7., Adams MA, Singh VK, Keller BO, Jia Z, Mol Microbiol. 2006 Sep;61(6):1469-84. Epub 2006 Aug 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16930152 16930152]
[[Category: Escherichia coli o127:h6]]
[[Category: Escherichia coli o127:h6]]
[[Category: Gentisate 1,2-dioxygenase]]
[[Category: Gentisate 1,2-dioxygenase]]
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[[Category: gentisic acid]]
[[Category: gentisic acid]]
[[Category: montreal-kingston bacterial structural genomics initiative]]
[[Category: montreal-kingston bacterial structural genomics initiative]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
[[Category: tetramer]]
[[Category: tetramer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:23:03 2008''

Revision as of 14:23, 20 March 2008


PDB ID 2d40

Drag the structure with the mouse to rotate
, resolution 2.41Å
Ligands:
Activity: Gentisate 1,2-dioxygenase, with EC number 1.13.11.4
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Z3393 from Escherichia coli O157:H7


Overview

Gentisic acid (2,5-dihydroxybenzoic acid) is a key intermediate in aerobic bacterial pathways that are responsible for the metabolism of a large number of aromatic compounds. The critical step of these pathways is the oxygen-dependent reaction catalysed by gentisate 1,2-dioxygenase which opens the aromatic ring of gentisate to form maleylpyruvate. From gentisic acid, the cell derives carbon and energy through the conversion of maleylpyruvate to central metabolites. We have confirmed the annotation of a gentisate 1,2-dioygenase from the pathogenic O157:H7 Escherichia coli strain and present the first structural characterization of this family of enzymes. The identity of the reaction product was revealed using tandem mass spectroscopy. The operon responsible for the degradation of gentisate in this organism exhibits a high degree of conservation with the gentisate-degrading operons of other pathogenic bacteria, including the Shiga toxin-producing E. coli O103:H2, but does not appear to be present in non-pathogenic strains. The acquisition of the gentisate operon may represent a special adaptation to meet carbon source requirements under conditions of environmental stress and may provide a selective advantage for enterohaemorrhagic E. coli relative to their non-pathogenic counterparts.

About this Structure

2D40 is a Single protein structure of sequence from Escherichia coli o127:h6. Full crystallographic information is available from OCA.

Reference

Structural and biochemical characterization of gentisate 1,2-dioxygenase from Escherichia coli O157:H7., Adams MA, Singh VK, Keller BO, Jia Z, Mol Microbiol. 2006 Sep;61(6):1469-84. Epub 2006 Aug 23. PMID:16930152

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