4PC7

Elongation factor Tu:Ts complex in a near GTP conformation.

Summary for 4PC7

• Entry DOI: 10.2210/pdb4pc7/pdb
• Related: 4PC1 4PC2 4PC3 4PC6
• Descriptor: Elongation factor Tu 1, Elongation factor Ts, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (6 entities in total)
• Functional Keywords: g:gef:nucleotide complex, elongation factor, translation, protein synthesis
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0CE47 P0A6P1
• Total number of polymer chains: 2
• Total formula weight: 75058.78

Authors

Thirup, S.S. (deposition date: 2014-04-14, release date: 2015-05-06, Last modification date: 2023-12-27)

Primary citation

Thirup, S.S.,Van, L.B.,Nielsen, T.K.,Knudsen, C.R.
Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu.
J.Struct.Biol., 191:10-21, 2015

PubMed 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.

PubMed: 26073967
DOI: 10.1016/j.jsb.2015.06.011

Experimental method

X-RAY DIFFRACTION (3.6003 Å)