2d40
From Proteopedia
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|PDB= 2d40 |SIZE=350|CAPTION= <scene name='initialview01'>2d40</scene>, resolution 2.41Å | |PDB= 2d40 |SIZE=350|CAPTION= <scene name='initialview01'>2d40</scene>, resolution 2.41Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene> | + | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d40 OCA], [http://www.ebi.ac.uk/pdbsum/2d40 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d40 RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2D40 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 2D40 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D40 OCA]. |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/16930152 16930152] | 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 | + | [[Category: Escherichia coli o157:h7]] |
[[Category: Gentisate 1,2-dioxygenase]] | [[Category: Gentisate 1,2-dioxygenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]] | [[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]] | ||
[[Category: Jia, Z.]] | [[Category: Jia, Z.]] | ||
| - | + | [[Category: 1,2-dioxygenase]] | |
| - | [[Category: 1 | + | |
| - | + | ||
[[Category: bicupin]] | [[Category: bicupin]] | ||
[[Category: bsgi]] | [[Category: bsgi]] | ||
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[[Category: tetramer]] | [[Category: tetramer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:30:03 2008'' |
Revision as of 23:30, 30 March 2008
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| , resolution 2.41Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Gentisate 1,2-dioxygenase, with EC number 1.13.11.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 o157:h7. 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
Page seeded by OCA on Mon Mar 31 02:30:03 2008
Categories: Escherichia coli o157:h7 | Gentisate 1,2-dioxygenase | Single protein | Adams, M A. | BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative. | Jia, Z. | 1,2-dioxygenase | Bicupin | Bsgi | Crystal structure | Gentisic acid | Montreal-kingston bacterial structural genomics initiative | Structural genomic | Tetramer
