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3hux

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3hux, resolution 3.10Å ()
Ligands: ,
Related: 3huw, 3huy, 3huz
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Contents

Structure of EF-P bound to the 70S ribosome; THIS FILE CONTAINS THE 50S SUBUNIT FOR MOLECULE I.

Publication Abstract from PubMed

Elongation factor P (EF-P) is an essential protein that stimulates the formation of the first peptide bond in protein synthesis. Here we report the crystal structure of EF-P bound to the Thermus thermophilus 70S ribosome along with the initiator transfer RNA N-formyl-methionyl-tRNA(i) (fMet-tRNA(i)(fMet)) and a short piece of messenger RNA (mRNA) at a resolution of 3.5 angstroms. EF-P binds to a site located between the binding site for the peptidyl tRNA (P site) and the exiting tRNA (E site). It spans both ribosomal subunits with its amino-terminal domain positioned adjacent to the aminoacyl acceptor stem and its carboxyl-terminal domain positioned next to the anticodon stem-loop of the P site-bound initiator tRNA. Domain II of EF-P interacts with the ribosomal protein L1, which results in the largest movement of the L1 stalk that has been observed in the absence of ratcheting of the ribosomal subunits. EF-P facilitates the proper positioning of the fMet-tRNA(i)(fMet) for the formation of the first peptide bond during translation initiation.

Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome., Blaha G, Stanley RE, Steitz TA, Science. 2009 Aug 21;325(5943):966-70. PMID:19696344

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3hux is a 31 chain structure with sequence from Thermus thermophilus. The January 2010 RCSB PDB Molecule of the Month feature on 70S Ribosomes by David Goodsell is 10.2210/rcsb_pdb/mom_2010_1. Full crystallographic information is available from OCA.

See Also

Reference

  • Blaha G, Stanley RE, Steitz TA. Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome. Science. 2009 Aug 21;325(5943):966-70. PMID:19696344 doi:325/5943/966

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