1tuv: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= ygiN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= ygiN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1r6y|1R6Y]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tuv OCA], [http://www.ebi.ac.uk/pdbsum/1tuv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tuv RCSB]</span> | |||
}} | }} | ||
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[[Category: Adams, M A.]] | [[Category: Adams, M A.]] | ||
[[Category: Jia, Z.]] | [[Category: Jia, Z.]] | ||
[[Category: co-crystal with natural product]] | [[Category: co-crystal with natural product]] | ||
[[Category: ferredoxin fold]] | [[Category: ferredoxin fold]] | ||
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[[Category: monooxygenase]] | [[Category: monooxygenase]] | ||
''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 00:01:23 2008'' | ||
Revision as of 21:01, 30 March 2008
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| 1tuv, resolution 1.70Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | VK3 | ||||||||||||
| Gene: | ygiN (Escherichia coli) | ||||||||||||
| Related: | 1R6Y
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| 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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