4D4Q

Crystal Structure of Kti13/AtS1

4D4Q の概要

• エントリーDOI: 10.2210/pdb4d4q/pdb
• 関連するPDBエントリー: 4D4O 4D4P
• 分子名称: PROTEIN ATS1 (2 entities in total)
• 機能のキーワード: translation, trna modification, diphthamide modification
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73832.88

構造登録者

Glatt, S.,Mueller, C.W. (登録日: 2014-10-30, 公開日: 2015-01-14, 最終更新日: 2024-10-23)

主引用文献

Glatt, S.,Zabel, R.,Vonkova, I.,Kumar, A.,Netz, D.J.,Pierik, A.J.,Rybin, V.,Lill, R.,Gavin, A.,Balbach, J.,Breunig, K.D.,Muller, C.W.
Structure of the Kti11/Kti13 Heterodimer and its Double Role in Modifications of tRNA and Eukaryotic Elongation Factor 2.
Structure, 23:7-, 2015

PubMed Abstract: 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.

PubMed: 25543256
DOI: 10.1016/J.STR.2014.11.008

実験手法

X-RAY DIFFRACTION (2.395 Å)