4PC3: Elongation factor Tu:Ts complex with partially bound GDP

Citation:
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 1.8A resolution), EF-Tu:PO4:EF-Ts (1.9A resolution), EF-Tu:GDPNP:EF-Ts (2.2A resolution) and EF-Tu:GDPNP:pulvomycin:Mg(2+):EF-Ts (3.5A 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.
PDB ID: 4PC3Download
MMDB ID: 129013
PDB Deposition Date: 2014/4/14
Updated in MMDB: 2018/07
Experimental Method:
x-ray diffraction
Resolution: 1.8313  Å
Source Organism:
Similar Structures:
Biological Unit for 4PC3: dimeric; determined by author and by software (PISA)
Molecular Components in 4PC3
Label Count Molecule
Proteins (2 molecules)
1
Elongation Factor TU 1(Gene symbol: tufA)
Molecule annotation
1
Elongation Factor TS(Gene symbol: tsf)
Molecule annotation
Chemicals (4 molecules)
1
1
2
3
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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