4x33
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/DPH3_YEAST DPH3_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.<ref>PMID:15485916</ref> [[http://www.uniprot.org/uniprot/ATS1_YEAST ATS1_YEAST]] May participate in regulatory interactions between microtubules and the cell cycle. | [[http://www.uniprot.org/uniprot/DPH3_YEAST DPH3_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.<ref>PMID:15485916</ref> [[http://www.uniprot.org/uniprot/ATS1_YEAST ATS1_YEAST]] May participate in regulatory interactions between microtubules and the cell cycle. | ||
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| + | == Publication Abstract from PubMed == | ||
| + | Modification of wobble uridines of many eukaryotic tRNAs requires the Elongator complex, a highly conserved six-subunit eukaryotic protein assembly, as well as the Killer toxin-insensitive (Kti) proteins 11-14. Kti11 was additionally shown to be implicated in the biosynthesis of diphthamide, a post-translationally modified histidine of translation elongation factor 2. Recent data indicate that iron-bearing Kti11 functions as an electron donor to the [4Fe-4S] cluster of radical S-Adenosylmethionine enzymes, triggering the subsequent radical reaction. We show here that recombinant yeast Kti11 forms a stable 1 : 1 complex with Kti13. To obtain insights into the function of this heterodimer, the Kti11/Kti13 complex was purified to homogeneity, crystallized, and its structure determined at 1.45 A resolution. The importance of several residues mediating complex formation was confirmed by mutagenesis. Kti13 adopts a fold characteristic of RCC1-like proteins. The seven-bladed beta-propeller consists of a unique mixture of four- and three-stranded blades. In the complex, Kti13 orients Kti11 and restricts access to its electron-carrying iron atom, constraining the electron transfer capacity of Kti11. Based on these findings, we propose a role for Kti13, and discuss the possible functional implications of complex formation. DATABASE: Structural data have been submitted to the Protein Data Bank under accession number 4X33. | ||
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| + | Structure of the Elongator cofactor complex Kti11/Kti13 provides insight into the role of Kti13 in Elongator-dependent tRNA modification.,Kolaj-Robin O, McEwen AG, Cavarelli J, Seraphin B FEBS J. 2015 Jan 21. doi: 10.1111/febs.13199. PMID:25604895<ref>PMID:25604895</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:54, 7 February 2015
Structure of the Elongator cofactor complex Kti11/Kti13 at 1.45A
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