PDBsum entry 4pc3

Translation

PDB id: 4pc3

Contents

Protein chains

363 a.a.

279 a.a.

Ligands

GDP ×2

GOL ×5

Waters ×1158

References listed in PDB file

Key reference

• Title: Structural outline of the detailed mechanism for elongation factor ts-Mediated guanine nucleotide exchange on elongation factor tu.
• Authors: S.S.Thirup, L.B.Van, T.K.Nielsen, C.R.Knudsen.
• Ref.: J Struct Biol, 2015, 191, 10-21. [DOI no: 10.1016/j.jsb.2015.06.011]
• PubMed id: 26073967

Abstract

Translation elongation factor EF-Tu belongs to the superfamily of guanine-nucleotide binding proteins, which play key cellular roles as regulatory switches. All G-proteins require activation via exchange of GDP for GTP to carry out their respective tasks. Often, guanine-nucleotide exchange factors are essential to this process. During translation, EF-Tu:GTP transports aminoacylated tRNA to the ribosome. GTP is hydrolyzed during this process, and subsequent reactivation of EF-Tu is catalyzed by EF-Ts. The reaction path of guanine-nucleotide exchange is structurally poorly defined for EF-Tu and EF-Ts. We have determined the crystal structures of the following reaction intermediates: two structures of EF-Tu:GDP:EF-Ts (2.2 and 1.8Å resolution), EF-Tu:PO4:EF-Ts (1.9Å resolution), EF-Tu:GDPNP:EF-Ts (2.2Å resolution) and EF-Tu:GDPNP:pulvomycin:Mg(2+):EF-Ts (3.5Å resolution). These structures provide snapshots throughout the entire exchange reaction and suggest a mechanism for the release of EF-Tu in its GTP conformation. An inferred sequence of events during the exchange reaction is presented.