PDBsum entry 4pc7

Translation

PDB id: 4pc7

Contents

Protein chains

367 a.a.

261 a.a.

Ligands

GNP

PUL

Metals

_MG

Waters ×1

PDB id:

4pc7

Name:

Translation

Title:

Elongation factor tu:ts complex in a near gtp conformation.

Structure:

Elongation factor tu 1. Chain: a. Synonym: ef-tu 1,p-43. Engineered: yes. Elongation factor ts. Chain: c. Synonym: ef-ts. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: tufa, b3339, jw3301. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: tsf, b0170, jw0165. Expression_system_taxid: 562

Resolution:

3.60Å R-factor: 0.257 R-free: 0.283

Authors:

S.S.Thirup

Key ref:

S.S.Thirup et al. (2015). Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu. J Struct Biol, 191, 10-21. PubMed id: 26073967 DOI: 10.1016/j.jsb.2015.06.011

Date:

14-Apr-14 Release date: 06-May-15

Protein chain

P0CE47  (EFTU1_ECOLI) -  Elongation factor Tu 1 from Escherichia coli (strain K12)

Seq: 394 a.a.

Struc: 367 a.a.

Protein chain

P0A6P1  (EFTS_ECOLI) -  Elongation factor Ts from Escherichia coli (strain K12)

Seq: 283 a.a.

Struc: 261 a.a.

DOI no: 10.1016/j.jsb.2015.06.011

J Struct Biol 191:10-21 (2015)

PubMed id: 26073967

Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu.

S.S.Thirup, L.B.Van, T.K.Nielsen, C.R.Knudsen.

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.