1TUI

INTACT ELONGATION FACTOR TU IN COMPLEX WITH GDP

Summary for 1TUI

• Entry DOI: 10.2210/pdb1tui/pdb
• Descriptor: ELONGATION FACTOR TU, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: elongation factor, protein biosynthesis, gtp-binding
• Biological source: Thermus aquaticus
• Cellular location: Cytoplasm: Q01698
• Total number of polymer chains: 3
• Total formula weight: 135631.46

Authors

Polekhina, G.,Thirup, S.,Kjeldgaard, M.,Nissen, P.,Lippmann, C.,Nyborg, J. (deposition date: 1996-05-23, release date: 1997-06-05, Last modification date: 2024-02-14)

Primary citation

Polekhina, G.,Thirup, S.,Kjeldgaard, M.,Nissen, P.,Lippmann, C.,Nyborg, J.
Helix unwinding in the effector region of elongation factor EF-Tu-GDP.
Structure, 4:1141-1151, 1996

PubMed Abstract: Elongation factor Tu (EF-Tu) in its GTP conformation is a carrier of aminoacylated tRNAs (aa-tRNAs) to the ribosomal A site during protein biosynthesis. The ribosome triggers GTP hydrolysis, resulting in the dissociation of EF-Tu-GDP from the ribosome. The affinity of EF-Tu for other molecules involved in this process, some of which are unknown, is regulated by two regions (Switch I and Switch II) that have different conformations in the GTP and GDP forms. The structure of the GDP form of EF-Tu is known only as a trypsin-modified fragment, which lacks the Switch I, or effector, domain. The aim of this work was to establish the overall structure of intact EF-Tu-GDP, in particular the structure of the effector domain.

PubMed: 8939739
DOI: 10.1016/S0969-2126(96)00122-0

Experimental method

X-RAY DIFFRACTION (2.7 Å)