4d4p
From Proteopedia
Crystal Structure of the Kti11 Kti13 heterodimer Spacegroup P65
Structural highlights
FunctionDPH3_YEAST Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2. Required for conferring sensitivity to K.lactis zymocin.[1] ATS1_YEAST May participate in regulatory interactions between microtubules and the cell cycle. Publication Abstract from PubMedThe small, highly conserved Kti11 alias Dph3 protein encoded by the Kluyveromyces lactis killer toxin insensitive gene KTI11/DPH3 is involved in the diphthamide modification of eukaryotic elongation factor 2 and, together with Kti13, in Elongator-dependent tRNA wobble base modifications, thereby affecting the speed and accuracy of protein biosynthesis through two distinct mechanisms. We have solved the crystal structures of Saccharomyces cerevisiae Kti13 and the Kti11/Kti13 heterodimer at 2.4 and 2.9 A resolution, respectively, and validated interacting residues through mutational analysis in vitro and in vivo. We show that metal coordination by Kti11 and its heterodimerization with Kti13 are essential for both translational control mechanisms. Our structural and functional analyses identify Kti13 as an additional component of the diphthamide modification pathway and provide insight into the molecular mechanisms that allow the Kti11/Kti13 heterodimer to coregulate two consecutive steps in ribosomal protein synthesis. Structure of the Kti11/Kti13 Heterodimer and Its Double Role in Modifications of tRNA and Eukaryotic Elongation Factor 2.,Glatt S, Zabel R, Vonkova I, Kumar A, Netz DJ, Pierik AJ, Rybin V, Lill R, Gavin AC, Balbach J, Breunig KD, Muller CW Structure. 2015 Jan 6;23(1):149-60. doi: 10.1016/j.str.2014.11.008. Epub 2014 Dec, 24. PMID:25543256[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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