Deoxyhypusine synthase

Function Deoxyhypusine synthase (DHS) catalyzes the biosynthesis of deoxyhypusine by transfer of 4-aminobutyl moiety of spermidine to a specific Lys residue of initiation factor 4D. Hypusine is formed post-translationally and is found in translation initiation factor 5A (elf5A). Disease Mutations in DHS result in reduced enzyme activity that limits the hypusination of elf5A which is associated with neurodevelopmental disorder. Relevance Inhibition of DHS may provide a strategy for reducing diabetogenic cells and preserving β cell function in type 1 diabetes. Structural highlights The hydrophobic groove of the FERM domain of Rdx binds the N-terminal peptide of the adhesion molecule P-selectin glycoprotein ligand 1 with multiple hydrogen bonds. Hydrophobic, Polar

spinqualitylabelsall models Mouse radixin FERM domain (green) complex with N-terminal peptide of the adhesion molecule PSGL-1 (yellow) (PDB code 2emt) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D Structures of deoxyhypusine synthase3D Structures of deoxyhypusine synthase

Updated on 04-February-2021

6xxh – hDHS – human
1dhs, 1rlz, 1roz, 6dft, 6xxi – hDHS + NAD
6xxm – hDHS + putrescine
6pgr, 6wkz, 6wl6 – hDHS + inhibitor
6xxl – hDHS + spermine
6xxk – hDHS + spermidine
6xxj – hDHS + NAD + spermidine
1rqd, 6prv – hDHS + NAD + inhibitor
7cmc – DHS + NAD - Pyrococcus horikishii
6w3z – DHS + NAD – Brugia malayi