6E0T
C-terminal domain of Fission Yeast OFD1
Summary for 6E0T
| Entry DOI | 10.2210/pdb6e0t/pdb |
| Descriptor | Prolyl 3,4-dihydroxylase ofd1 (2 entities in total) |
| Functional Keywords | prolyl hydrolase sterol synthesis, cytosolic protein |
| Biological source | Schizosaccharomyces pombe (Fission yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 30374.28 |
| Authors | Bianchet, M.A.,Amzel, L.M.,Espenshade, P.J.,Yeh, T. (deposition date: 2018-07-06, release date: 2019-09-11, Last modification date: 2024-03-13) |
| Primary citation | Yeh, T.L.,Lee, C.Y.,Amzel, L.M.,Espenshade, P.J.,Bianchet, M.A. The hypoxic regulator of sterol synthesis nro1 is a nuclear import adaptor. Structure, 19:503-514, 2011 Cited by PubMed Abstract: Fission yeast protein Sre1, the homolog of the mammalian sterol regulatory element-binding protein (SREBP), is a hypoxic transcription factor required for sterol homeostasis and low-oxygen growth. Nro1 regulates the stability of the N-terminal transcription factor domain of Sre1 (Sre1N) by inhibiting the action of the prolyl 4-hydroxylase-like Ofd1 in an oxygen-dependent manner. The crystal structure of Nro1 determined at 2.2 Å resolution shows an all-α-helical fold that can be divided into two domains: a small N-terminal domain, and a larger C-terminal HEAT-repeat domain. Follow-up studies showed that Nro1 defines a new class of nuclear import adaptor that functions both in Ofd1 nuclear localization and in the oxygen-dependent inhibition of Ofd1 to control the hypoxic response. PubMed: 21481773DOI: 10.1016/j.str.2011.01.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.02 Å) |
Structure validation
Download full validation report
