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4N9Q

Crystal structure of paAzoR1 bound to ubiquinone-1

Summary for 4N9Q
Entry DOI10.2210/pdb4n9q/pdb
Related2V9C 3KEG 3R6W 4N65
DescriptorFMN-dependent NADH-azoreductase 1, FLAVIN MONONUCLEOTIDE, UBIQUINONE-1, ... (6 entities in total)
Functional Keywordsazoreductase, quinone, nad(p)h quinone oxidoreductase, ubiquinone-1, oxidoreductase
Biological sourcePseudomonas aeruginosa
Total number of polymer chains2
Total formula weight47505.28
Authors
Ryan, A.,Kaplan, E.,Crescente, V.,Lowe, E.,Preston, G.M.,Sim, E. (deposition date: 2013-10-21, release date: 2014-06-11, Last modification date: 2023-09-20)
Primary citationRyan, A.,Kaplan, E.,Nebel, J.C.,Polycarpou, E.,Crescente, V.,Lowe, E.,Preston, G.M.,Sim, E.
Identification of NAD(P)H Quinone Oxidoreductase Activity in Azoreductases from P. aeruginosa: Azoreductases and NAD(P)H Quinone Oxidoreductases Belong to the Same FMN-Dependent Superfamily of Enzymes.
Plos One, 9:e98551-e98551, 2014
Cited by
PubMed Abstract: Water soluble quinones are a group of cytotoxic anti-bacterial compounds that are secreted by many species of plants, invertebrates, fungi and bacteria. Studies in a number of species have shown the importance of quinones in response to pathogenic bacteria of the genus Pseudomonas. Two electron reduction is an important mechanism of quinone detoxification as it generates the less toxic quinol. In most organisms this reaction is carried out by a group of flavoenzymes known as NAD(P)H quinone oxidoreductases. Azoreductases have previously been separate from this group, however using azoreductases from Pseudomonas aeruginosa we show that they can rapidly reduce quinones. Azoreductases from the same organism are also shown to have distinct substrate specificity profiles allowing them to reduce a wide range of quinones. The azoreductase family is also shown to be more extensive than originally thought, due to the large sequence divergence amongst its members. As both NAD(P)H quinone oxidoreductases and azoreductases have related reaction mechanisms it is proposed that they form an enzyme superfamily. The ubiquitous and diverse nature of azoreductases alongside their broad substrate specificity, indicates they play a wide role in cellular survival under adverse conditions.
PubMed: 24915188
DOI: 10.1371/journal.pone.0098551
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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数据于2024-11-06公开中

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