Structural highlights
4pc6 is a 4 chain structure with sequence from Ecod1 and Ecodh. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Related: | 4pc1, 4pc2, 4pc3 |
| Gene: | tufA, tuf, ECDH10B_3514 (ECODH), tsf, EcDH1_3433, ECDH1ME8569_0163 (ECOD1) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[B1X6I9_ECODH] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] [C9QRL8_ECOD1] Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.[HAMAP-Rule:MF_00050][RuleBase:RU000642]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Thirup SS, Van LB, Nielsen TK, Knudsen CR. Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu. J Struct Biol. 2015 Jun 11. pii: S1047-8477(15)30015-0. doi:, 10.1016/j.jsb.2015.06.011. PMID:26073967 doi:http://dx.doi.org/10.1016/j.jsb.2015.06.011
