ArticleStructure (London, England : 1993)2015
Structure of the ribosomal oxygenase OGFOD1 provides insights into the regio- and stereoselectivity of prolyl hydroxylases.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- OGFOD1: a critical mediator of chemoresistance in acute myeloid leukemia.Frontiers in pharmacology · 2026Article
- Time-resolved NMR detection of prolyl-hydroxylation in intrinsically disordered region of HIF-1α.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Recent Advances and Therapeutic Implications of 2-Oxoglutarate-Dependent Dioxygenases in Ischemic Stroke.Molecular neurobiology · 2024Review
- Inhibition of OGFOD1 by FG4592 confers neuroprotection by activating unfolded protein response and autophagy after ischemic stroke.Journal of translational medicine · 2024Article
- Ogfod1 deletion increases cardiac beta-alanine levels and protects mice against ischaemia- reperfusion injury.Cardiovascular research · 2022Article
- Iron in Translation: From the Beginning to the End.Microorganisms · 2021Review
- Use of cyclic peptides to induce crystallization: case study with prolyl hydroxylase domain 2.Scientific reports · 2020Article
- Biochemical and biophysical analyses of hypoxia sensing prolyl hydroxylases fromThe Journal of biological chemistry · 2020Article
- Structure-Activity Relationship and Crystallographic Studies on 4-Hydroxypyrimidine HIF Prolyl Hydroxylase Domain Inhibitors.ChemMedChem · 2020Article
- Expansion of base excision repair compensates for a lack of DNA repair by oxidative dealkylation in budding yeast.The Journal of biological chemistry · 2019Article
- Oxygen-dependent bond formation with FIH regulates the activity of the client protein OTUB1.Redox biology · 2019Article
- Biochemical and structural investigations clarify the substrate selectivity of the 2-oxoglutarate oxygenase JMJD6.The Journal of biological chemistry · 2019Article
- Selective Inhibitors of a Human Prolyl Hydroxylase (OGFOD1) Involved in Ribosomal Decoding.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3.Nature communications · 2018Article
- Amazing Diversity in Biochemical Roles of Fe(II)/2-Oxoglutarate Oxygenases.Trends in biochemical sciences · 2018Review
- Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by FeNature communications · 2018Article
- Molecular and cellular mechanisms of HIF prolyl hydroxylase inhibitors in clinical trials.Chemical science · 2017Article
- Bacillus anthracis Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu.Biochemistry · 2017Article
- Article
- Bacillus anthracis Prolyl 4-Hydroxylase Modifies Collagen-like Substrates in Asymmetric Patterns.The Journal of biological chemistry · 2016Article
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
Post-translational ribosomal protein hydroxylation is catalyzed by 2-oxoglutarate (2OG) and ferrous iron dependent oxygenases, and occurs in prokaryotes and eukaryotes. OGFOD1 catalyzes trans-3 prolyl hydroxylation at Pro62 of the small ribosomal subunit protein uS12 (RPS23) and is conserved from yeasts to humans. We describe crystal structures of the human uS12 prolyl 3-hydroxylase (OGFOD1) and its homolog from Saccharomyces cerevisiae (Tpa1p): OGFOD1 in complex with the broad-spectrum 2OG oxygenase inhibitors; N-oxalylglycine (NOG) and pyridine-2,4-dicarboxylate (2,4-PDCA) to 2.1 and 2.6 Å resolution, respectively; and Tpa1p in complex with NOG, 2,4-PDCA, and 1-chloro-4-hydroxyisoquinoline-3-carbonylglycine (a more selective prolyl hydroxylase inhibitor) to 2.8, 1.9, and 1.9 Å resolution, respectively. Comparison of uS12 hydroxylase structures with those of other prolyl hydroxylases, including the human hypoxia-inducible factor (HIF) prolyl hydroxylases (PHDs), reveals differences between the prolyl 3- and prolyl 4-hydroxylase active sites, which can be exploited for developing selective inhibitors of the different subfamilies.
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