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3dwu
From Proteopedia
Revision as of 17:18, 10 April 2020 by OCA (Talk | contribs)
3dwu is a 1 chain structure with sequence from Thermus thermophilus hb8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[EFTU2_THET8] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Evolutionary Conservation
Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In an attempt to understand ribosome-induced GTP hydrolysis on eEF2, we determined a 12.6-A cryo-electron microscopy reconstruction of the eEF2-bound 80S ribosome in the presence of aluminum tetrafluoride and GDP, with aluminum tetrafluoride mimicking the gamma-phosphate during hydrolysis. This is the first visualization of a structure representing a transition-state complex on the ribosome. Tight interactions are observed between the factor's G domain and the large ribosomal subunit, as well as between domain IV and an intersubunit bridge. In contrast, some of the domains of eEF2 implicated in small subunit binding display a large degree of flexibility. Furthermore, we find support for a transition-state model conformation of the switch I region in this complex where the reoriented switch I region interacts with a conserved rRNA region of the 40S subunit formed by loops of the 18S RNA helices 8 and 14. This complex is structurally distinct from the eEF2-bound 80S ribosome complexes previously reported, and analysis of this map sheds light on the GTPase-coupled translocation mechanism.
Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy.,Sengupta J, Nilsson J, Gursky R, Kjeldgaard M, Nissen P, Frank J J Mol Biol. 2008 Sep 26;382(1):179-87. Epub 2008 Jul 11. PMID:18644383[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
