4pc1 | pdb_00004pc1

Elongation Factor Tu:Ts complex with a bound phosphate

spinqualitylabelsall models 4pc1, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pc1 is a 4 chain structure with sequence from Escherichia coli and Escherichia coli str. K-12 substr. DH10B. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, PB, PO4, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0M3KKV1_ECODH This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] Publication Abstract from PubMed 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:Mg2+: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. Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu.,Thirup SS, Van LB, Nielsen TK, Knudsen CR J Struct Biol. 2015 Jun 11. pii: S1047-8477(15)30015-0. doi:, 10.1016/j.jsb.2015.06.011. PMID:26073967 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures

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