1tuv
From Proteopedia
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| - | [[Image:1tuv.gif|left|200px]] | + | [[Image:1tuv.gif|left|200px]] |
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| - | '''Crystal structure of YgiN in complex with menadione''' | + | {{Structure |
| + | |PDB= 1tuv |SIZE=350|CAPTION= <scene name='initialview01'>1tuv</scene>, resolution 1.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=VK3:MENADIONE'>VK3</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= ygiN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of YgiN in complex with menadione''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TUV is a [ | + | 1TUV 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=1TUV OCA]. |
==Reference== | ==Reference== | ||
| - | Structural and biochemical evidence for an enzymatic quinone redox cycle in Escherichia coli: identification of a novel quinol monooxygenase., Adams MA, Jia Z, J Biol Chem. 2005 Mar 4;280(9):8358-63. Epub 2004 Dec 21. PMID:[http:// | + | Structural and biochemical evidence for an enzymatic quinone redox cycle in Escherichia coli: identification of a novel quinol monooxygenase., Adams MA, Jia Z, J Biol Chem. 2005 Mar 4;280(9):8358-63. Epub 2004 Dec 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15613473 15613473] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: monooxygenase]] | [[Category: monooxygenase]] | ||
| - | ''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 14:23:29 2008'' |
Revision as of 12:23, 20 March 2008
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| , resolution 1.70Å | |||||||
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| Ligands: | |||||||
| Gene: | ygiN (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of YgiN in complex with menadione
Overview
Naturally synthesized quinones perform a variety of important cellular functions. Escherichia coli produce both ubiquinone and menaquinone, which are involved in electron transport. However, semiquinone intermediates produced during the one-electron reduction of these compounds, as well as through auto-oxidation of the hydroxyquinone product, generate reactive oxygen species that stress the cell. Here, we present the crystal structure of YgiN, a protein of hitherto unknown function. The three-dimensional fold of YgiN is similar to that of ActVA-Orf6 monooxygenase, which acts on hydroxyquinone substrates. YgiN shares a promoter with "modulator of drug activity B," a protein with activity similar to that of mammalian DT-diaphorase capable of reducing mendione. YgiN was able to reoxidize menadiol, the product of the "modulator of drug activity B" (MdaB) enzymatic reaction. We therefore refer to YgiN as quinol monooxygenase. Modulator of drug activity B is reported to be involved in the protection of cells from reactive oxygen species formed during single electron oxidation and reduction reactions. The enzymatic activities, together with the structural characterization of YgiN, lend evidence to the possible existence of a novel quinone redox cycle in E. coli.
About this Structure
1TUV is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural and biochemical evidence for an enzymatic quinone redox cycle in Escherichia coli: identification of a novel quinol monooxygenase., Adams MA, Jia Z, J Biol Chem. 2005 Mar 4;280(9):8358-63. Epub 2004 Dec 21. PMID:15613473
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