3DWU

Transition-state model conformation of the switch I region fitted into the cryo-EM map of the eEF2.80S.AlF4.GDP complex

3DWU の概要

• エントリーDOI: 10.2210/pdb3dwu/pdb
• 関連するPDBエントリー: 1AS2 1N0U 3DNY
• EMDBエントリー: 5015
• 分子名称: Elongation factor Tu-B (1 entity in total)
• 機能のキーワード: transition state, conserved switch i, antibiotic resistance, elongation factor, gtp-binding, membrane, methylation, nucleotide-binding, phosphoprotein, protein biosynthesis, biosynthetic protein
• 由来する生物種: Thermus thermophilus HB8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4949.44

構造登録者

Nissen, P.,Nyborg, J.,Kjeldgaard, M. (登録日: 2008-07-23, 公開日: 2008-08-12, 最終更新日: 2024-02-21)

主引用文献

Sengupta, J.,Nilsson, J.,Gursky, R.,Kjeldgaard, M.,Nissen, P.,Frank, J.
Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy.
J.Mol.Biol., 382:179-187, 2008

PubMed Abstract: In an attempt to understand ribosome-induced GTP hydrolysis on eEF2, we determined a 12.6-A cryo-electron microscopy reconstruction of the eEF2-bound 80S ribosome in the presence of aluminum tetrafluoride and GDP, with aluminum tetrafluoride mimicking the gamma-phosphate during hydrolysis. This is the first visualization of a structure representing a transition-state complex on the ribosome. Tight interactions are observed between the factor's G domain and the large ribosomal subunit, as well as between domain IV and an intersubunit bridge. In contrast, some of the domains of eEF2 implicated in small subunit binding display a large degree of flexibility. Furthermore, we find support for a transition-state model conformation of the switch I region in this complex where the reoriented switch I region interacts with a conserved rRNA region of the 40S subunit formed by loops of the 18S RNA helices 8 and 14. This complex is structurally distinct from the eEF2-bound 80S ribosome complexes previously reported, and analysis of this map sheds light on the GTPase-coupled translocation mechanism.

PubMed: 18644383
DOI: 10.1016/j.jmb.2008.07.004

実験手法

ELECTRON MICROSCOPY (12.6 Å)