ArticleInternational journal of molecular sciences2014
Structural data on the periplasmic aldehyde oxidoreductase PaoABC from Escherichia coli: SAXS and preliminary X-ray crystallography analysis.
Article in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Biocompatible α-Methylenation of Metabolic Butyraldehyde in Living Bacteria.Angewandte Chemie (International ed. in English) · 2023Article
- Isolation of full-length IgG antibodies from combinatorial libraries expressed in the cytoplasm of Escherichia coli.Nature communications · 2023Article
- Molybdenum Enzymes and How They Support Virulence in Pathogenic Bacteria.Frontiers in microbiology · 2020Review
- Trees, fungi and bacteria: tripartite metatranscriptomics of a root microbiome responding to soil contamination.Microbiome · 2018Article
- The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria.Biochimica et biophysica acta · 2015Review
- An engineered genetic selection for ternary protein complexes inspired by a natural three-component hitchhiker mechanism.Scientific reports · 2014Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The periplasmic aldehyde oxidoreductase PaoABC from Escherichia coli is a molybdenum enzyme involved in detoxification of aldehydes in the cell. It is an example of an αβγ heterotrimeric enzyme of the xanthine oxidase family of enzymes which does not dimerize via its molybdenum cofactor binding domain. In order to structurally characterize PaoABC, X-ray crystallography and small angle X-ray scattering (SAXS) have been carried out. The protein crystallizes in the presence of 20% (w/v) polyethylene glycol 3350 using the hanging-drop vapour diffusion method. Although crystals were initially twinned, several experiments were done to overcome twinning and lowering the crystallization temperature (293 K to 277 K) was the solution to the problem. The non-twinned crystals used to solve the structure diffract X-rays to beyond 1.80 Å and belong to the C2 space group, with cell parameters a = 109.42 Å, b = 78.08 Å, c = 151.77 Å, β = 99.77°, and one molecule in the asymmetric unit. A molecular replacement solution was found for each subunit separately, using several proteins as search models. SAXS data of PaoABC were also collected showing that, in solution, the protein is also an αβγ heterotrimer.
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