4v5g
From Proteopedia
The crystal structure of the 70S ribosome bound to EF-Tu and tRNA
Structural highlights
FunctionRL1_THET8 Directly binds to 23S rRNA. Forms what is known as the L1 stalk, which protrudes beyond the 70S ribosome surface. The stalk is preferentially stabilized in 70S versus 50S crystals. Interacts with the E site tRNA, blocking the exit path. This blockage implies that this section of the ribosome must be able to move to release the deacetylated tRNA.[HAMAP-Rule:MF_01318_B] Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).[HAMAP-Rule:MF_01318_B] Publication Abstract from PubMedThe ribosome selects a correct transfer RNA (tRNA) for each amino acid added to the polypeptide chain, as directed by messenger RNA (mRNA). Aminoacyl-tRNA is delivered to the ribosome by elongation factor Tu (EF-Tu), which hydrolyzes guanosine triphosphate (GTP) and releases tRNA in response to codon recognition. The signaling pathway that leads to GTP hydrolysis upon codon recognition is critical to accurate decoding. Here, we present the crystal structure of the ribosome complexed with EF-Tu and aminoacyl-tRNA, refined to 3.6 angstrom resolution. The structure reveals details of the tRNA distortion that allows aminoacyl-tRNA to interact simultaneously with the decoding center of the 30S subunit and EF-Tu at the factor-binding site. A series of conformational changes in EF-Tu and aminoacyl-tRNA suggest a communication pathway between the decoding center and the guanosine triphosphatase center of EF-Tu. The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA.,Schmeing TM, Voorhees RM, Kelley AC, Gao YG, Murphy FV 4th, Weir JR, Ramakrishnan V Science. 2009 Oct 15. PMID:19833920[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
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