Journal
STRUCTURE
Volume 23, Issue 5, Pages 882-892Publisher
CELL PRESS
DOI: 10.1016/j.str.2015.03.002
Keywords
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Funding
- German Federal Ministry of Education and Research (BMBF) [01GUO718]
- DFG Cluster of Excellence Inflammation at Interfaces'' [EXC 206]
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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 (hDOHH(peroxo)) when its reduced form reacts with O-2. hDOHH(peroxo) has a lifetime exceeding that of the peroxo intermediates of other diiron enzymes by several orders of magnitude. Here we report the 1.7-angstrom crystal structures of hDOHH(peroxo) and a complex with glycerol. The structure of hDOHH(peroxo) reveals the presence of a mu-1,2-peroxo-diiron(III) species at the active site. Augmented by UV/Vis and Mossbauer spectroscopic studies, the crystal structures offer explanations for the extreme longevity of hDOHH(peroxo) and illustrate how the enzyme specifically recognizes its only substrate, deoxyhypusine-eIF-5A.
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