6ji2

Crystal structure of archaeal ribosomal protein aP1, aPelota, and GTP-bound aEF1A complex

spinqualitylabelsall models 6ji2, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ji2 is a 5 chain structure with sequence from Aeropyrum pernix K1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: GTP, MG, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EF1A_AERPE This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (By similarity). Publication Abstract from PubMed Translation elongation factor EF1A delivers aminoacyl-tRNA to the ribosome in a GTP-bound form, and is released from the ribosome in a GDP-bound form. This association/dissociation cycle proceeds efficiently via a marked conformational change in EF1A. EF1A function is dependent on the ribosomal "stalk" protein of the ribosomal large subunit, although the precise mechanism of action of the stalk on EF1A remains unclear. Here, we clarify the binding mode of archaeal stalk aP1 to GTP-bound aEF1A associated with aPelota. Intriguingly, the C-terminal domain (CTD) of aP1 binds to aEF1A*GTP with a similar affinity to aEF1A*GDP. We have also determined the crystal structure of the aP1-CTD*aEF1A*GTP*aPelota complex at 3.0 A resolution. The structure shows that aP1-CTD binds to a space between domains 1 and 3 of aEF1A. Biochemical analyses show that this binding is crucial for protein synthesis. Comparison of the structures of aP1-CTD*aEF1A*GTP and aP1-CTD*aEF1A*GDP demonstrates that the binding mode of aP1 changes markedly upon a conformational switch between the GTP- and GDP-bound forms of aEF1A. Taking into account biochemical data, we infer that aP1 employs its structural flexibility to bind to aEF1A before and after GTP hydrolysis for efficient protein synthesis. Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations.,Maruyama K, Imai H, Kawamura M, Ishino S, Ishino Y, Ito K, Uchiumi T Sci Rep. 2019 Oct 14;9(1):14761. doi: 10.1038/s41598-019-51266-x. PMID:31611569 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures

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