ArticleActa crystallographica. Section F, Structural biology communications2018
T4 lysozyme-facilitated crystallization of the human molybdenum cofactor-dependent enzyme mARC.
Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- The History of mARC.Molecules (Basel, Switzerland) · 2023Review
- From the Eukaryotic Molybdenum Cofactor Biosynthesis to the Moonlighting Enzyme mARC.Molecules (Basel, Switzerland) · 2018Review
- Crystal structure of human mARC1 reveals its exceptional position among eukaryotic molybdenum enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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Authors and funding
6 authors at 4 institutions in 1 country.
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Abstract
The human mitochondrial amidoxime reducing component (hmARC) is a molybdenum cofactor-dependent enzyme that is involved in the reduction of a diverse range of N-hydroxylated compounds of either physiological or xenobiotic origin. In this study, the use of a fusion-protein approach with T4 lysozyme (T4L) to determine the structure of this hitherto noncrystallizable enzyme by X-ray crystallography is described. A set of four different hmARC-T4L fusion proteins were designed. Two of them contained either an N-terminal or a C-terminal T4L moiety fused to hmARC, while the other two contained T4L as an internal fusion partner tethered to the hmARC enzyme between two predicted secondary-structure elements. One of these internal fusion constructs could be expressed and crystallized successfully. The hmARC-T4L crystals diffracted to 1.7 Å resolution using synchrotron radiation and belonged to space group P2
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