| Reference : Structure of the ribosomal oxygenase OGFOD1 provides insights into the regio- and ste... |
| Scientific journals : Article | |||
| Life sciences : Biochemistry, biophysics & molecular biology | |||
| http://hdl.handle.net/10993/26337 | |||
| Structure of the ribosomal oxygenase OGFOD1 provides insights into the regio- and stereoselectivity of prolyl hydroxylases. | |
| English | |
| Horita, Shoichiro [> >] | |
| Scotti, John S. [> >] | |
| Thinnes, Cyrille [University of Oxford > Department of Chemistry] | |
| Mottaghi-Taromsari, Yousef S. [> >] | |
| Thalhammer, Armin [> >] | |
| Ge, Wei [> >] | |
| Aik, Weishen [> >] | |
| Loenarz, Christoph [> >] | |
| Schofield, Christopher J. [> >] | |
| McDonough, Michael A. [> >] | |
| 2015 | |
| Structure (London, England : 1993) | |
| 23 | |
| 4 | |
| 639-52 | |
| Yes (verified by ORBilu) | |
| International | |
| 0969-2126 | |
| 1878-4186 | |
| United States | |
| [en] Amino Acid Sequence ; Binding Sites ; Carrier Proteins/antagonists & inhibitors/chemistry/metabolism ; Humans ; Molecular Docking Simulation ; Molecular Sequence Data ; Nuclear Proteins/antagonists & inhibitors/chemistry/metabolism ; Prolyl-Hydroxylase Inhibitors/pharmacology ; Protein Binding ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins/antagonists & inhibitors/chemistry/metabolism ; Substrate Specificity | |
| [en] 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 A 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 A 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. | |
| http://hdl.handle.net/10993/26337 | |
| Copyright (c) 2015 The Authors. Published by Elsevier Ltd.. All rights reserved. |
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