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PDBsum entry 4d4p
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Contents |
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413 a.a.
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336 a.a.
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76 a.a.
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References listed in PDB file
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Key reference
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Title
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Structure of the kti11/kti13 heterodimer and its double role in modifications of tRNA and eukaryotic elongation factor 2.
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Authors
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S.Glatt,
R.Zabel,
I.Vonkova,
A.Kumar,
D.J.Netz,
A.J.Pierik,
V.Rybin,
R.Lill,
A.C.Gavin,
J.Balbach,
K.D.Breunig,
C.W.Müller.
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Ref.
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Structure, 2015,
23,
149-160.
[DOI no: ]
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PubMed id
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Abstract
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The 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 Å 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.
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