2l6l

Structural highlights

Function

[DJC24_HUMAN] Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron-bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta).^{[1] [2]}

References

1. ↑ Wei H, Xiang L, Wayne AS, Chertov O, FitzGerald DJ, Bera TK, Pastan I. Immunotoxin resistance via reversible methylation of the DPH4 promoter is a unique survival strategy. Proc Natl Acad Sci U S A. 2012 May 1;109(18):6898-903. doi:, 10.1073/pnas.1204523109. Epub 2012 Apr 16. PMID:22509046 doi:http://dx.doi.org/10.1073/pnas.1204523109
2. ↑ Thakur A, Chitoor B, Goswami AV, Pareek G, Atreya HS, D'Silva P. Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4. J Biol Chem. 2012 Apr 13;287(16):13194-205. Epub 2012 Feb 24. PMID:22367199 doi:http://dx.doi.org/10.1074/jbc.M112.339655