Figures & data
Figure 1 Overview of the HIF system.
Abbreviations: PHD, Prolyl hydroxylases; HIF, hypoxia-inducible transcription factor; ODD, oxygen-dependent degradation domain; bHLH, basic helix-loop-helix motif; PAS, Per-ARNT-Sim domain; CTAD, C-terminal transactivation domain; PAC, PAS-associated C-terminal domain; FIH, factor inhibiting HIF.
![Figure 1 Overview of the HIF system.](/cms/asset/1249703c-96e1-4250-8b05-c557a9841c0e/dhpx_a_12195785_f0001_c.jpg)
Figure 2 Evidence for conservation of biochemical properties between TaPHD and HsPHD2.
![Figure 2 Evidence for conservation of biochemical properties between TaPHD and HsPHD2.](/cms/asset/fdaa69a0-ba07-458c-9ba0-84a0ec3eea28/dhpx_a_12195785_f0002_c.jpg)
Table 1 Data collection and refinement statistics
Figure 3 Views from crystal structures of the Trichoplax adhaerens prolyl hydroxylases (PHD) without substrate bound (TaPHD) and in complex with a fragment of its substrate (TaPHD.TaODD).
![Figure 3 Views from crystal structures of the Trichoplax adhaerens prolyl hydroxylases (PHD) without substrate bound (TaPHD) and in complex with a fragment of its substrate (TaPHD.TaODD).](/cms/asset/1e5d020f-e46e-46d6-826e-640398551a68/dhpx_a_12195785_f0003_c.jpg)
Figure 4 Comparison of ODD binding modes by the T. adhaerens and human HIFα PHD for the TaPHD.TaODD, HsPHD2.CODD and HsPHD2.NODD substrate structures.
Abbreviations: T. adhaerens, Trichoplax adhaerens; ODD, oxygen dependent degradation domain.
![Figure 4 Comparison of ODD binding modes by the T. adhaerens and human HIFα PHD for the TaPHD.TaODD, HsPHD2.CODD and HsPHD2.NODD substrate structures.](/cms/asset/dedc90c9-25e9-4897-90ad-4c8c5be90182/dhpx_a_12195785_f0004_c.jpg)
Figure 5 Comparison of substrate binding modes by TaPHD, CrP4H and Pseudomonas putida PPHD.
![Figure 5 Comparison of substrate binding modes by TaPHD, CrP4H and Pseudomonas putida PPHD.](/cms/asset/3fcc7926-762f-4c44-bd28-365edd827660/dhpx_a_12195785_f0005_c.jpg)
Figure 6 Active site metal region details and comparison of the conformations of the target prolyl-residues in the enzyme-substrate complex structures of TaPHD, HsPHD2, PPHD, and CrP4H.
![Figure 6 Active site metal region details and comparison of the conformations of the target prolyl-residues in the enzyme-substrate complex structures of TaPHD, HsPHD2, PPHD, and CrP4H.](/cms/asset/9522bc8f-fb24-4236-9958-bb220cc41497/dhpx_a_12195785_f0006_c.jpg)