2Y33
S-nitrosylated PHD2 (GSNO soaked) in complex with Zn(II) and UN9
Summary for 2Y33
| Entry DOI | 10.2210/pdb2y33/pdb |
| Related | 2G19 2G1M 2HBT 2HBU 2Y34 |
| Descriptor | EGL NINE HOMOLOG 1, ZINC ION, N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, non-heme, transcription and epigenetic regulation |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 28472.01 |
| Authors | Chowdhury, R.,Clifton, I.J.,Schofield, C.J. (deposition date: 2010-12-18, release date: 2010-12-29, Last modification date: 2024-10-09) |
| Primary citation | Chowdhury, R.,Flashman, E.,Mecinovic, J.,Kramer, H.B.,Kessler, B.M.,Frapart, Y.M.,Boucher, J.-L.,Clifton, I.J.,McDonough, M.A.,Schofield, C.J. Studies on the Reaction of Nitric Oxide with the Hypoxia-Inducible Factor Prolyl Hydroxylase Domain 2 (Egln1) J.Mol.Biol., 410:268-279, 2011 Cited by PubMed Abstract: The hypoxic response in animals is mediated via the transcription factor hypoxia-inducible factor (HIF). An oxygen-sensing component of the HIF system is provided by Fe(II) and 2-oxoglutarate-dependent oxygenases that catalyse the posttranslational hydroxylation of the HIF-α subunit. It is proposed that the activity of the HIF hydroxylases can be regulated by their reaction with nitric oxide. We describe biochemical and biophysical studies on the reaction of prolyl hydroxylase domain-containing enzyme (PHD) isoform 2 (EGLN1) with nitric oxide and a nitric oxide transfer reagent. The combined results reveal the potential for the catalytic domain of PHD2 to react with nitric oxide both at its Fe(II) and at cysteine residues. Although the biological significance is unclear, the results suggest that the reaction of PHD2 with nitric oxide has the potential to be complex and are consistent with proposals based on cellular studies that nitric oxide may regulate the hypoxic response by direct reaction with the HIF hydroxylases. PubMed: 21601578DOI: 10.1016/J.JMB.2011.04.075 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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