4D50

Structure of human deoxyhypusine hydroxylase

Summary for 4D50

• Entry DOI: 10.2210/pdb4d50/pdb
• Related: 4D4Z
• Descriptor: DEOXYHYPUSINE HYDROXYLASE, FE (III) ION, PEROXIDE ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 64565.07

Authors

Han, Z.,Sakai, N.,Hilgenfeld, R. (deposition date: 2014-10-31, release date: 2015-04-15, Last modification date: 2024-05-08)

Primary citation

Han, Z.,Sakai, N.,Bottger, L.H.,Klinke, S.,Hauber, J.,Trautwein, A.X.,Hilgenfeld, R.
Crystal Structure of the Peroxo-Diiron(III) Intermediate of Deoxyhypusine Hydroxylase, an Oxygenase Involved in Hypusination.
Structure, 23:882-, 2015

PubMed Abstract: Deoxyhypusine hydroxylase (DOHH) is a non-heme diiron enzyme involved in the posttranslational modification of a critical lysine residue of eukaryotic translation initiation factor 5A (eIF-5A) to yield the unusual amino acid residue hypusine. This modification is essential for the role of eIF-5A in translation and in nuclear export of a group of specific mRNAs. The diiron center of human DOHH (hDOHH) forms a peroxo-diiron(III) intermediate (hDOHHperoxo) when its reduced form reacts with O2. hDOHHperoxo has a lifetime exceeding that of the peroxo intermediates of other diiron enzymes by several orders of magnitude. Here we report the 1.7-Å crystal structures of hDOHHperoxo and a complex with glycerol. The structure of hDOHHperoxo reveals the presence of a μ-1,2-peroxo-diiron(III) species at the active site. Augmented by UV/Vis and Mössbauer spectroscopic studies, the crystal structures offer explanations for the extreme longevity of hDOHHperoxo and illustrate how the enzyme specifically recognizes its only substrate, deoxyhypusine-eIF-5A.

PubMed: 25865244
DOI: 10.1016/J.STR.2015.03.002

Experimental method

X-RAY DIFFRACTION (1.7 Å)