2XL1

Structural basis of translational stalling by human cytomegalovirus (hCMV) and fungal arginine attenuator peptide (AAP)

Summary for 2XL1

• Entry DOI: 10.2210/pdb2xl1/pdb
• Descriptor: ARGININE ATTENUATOR PEPTIDE (1 entity in total)
• Functional Keywords: translation, antibiotic, ribosome, cytomegalovirus
• Biological source: NEUROSPORA CRASSA
• Total number of polymer chains: 1
• Total formula weight: 2782.08

Authors

Meyer, N.H.,Sattler, M. (deposition date: 2010-07-15, release date: 2010-10-20, Last modification date: 2024-05-15)

Primary citation

Bhushan, S.,Meyer, H.,Starosta, A.L.,Becker, T.,Mielke, T.,Berninghausen, O.,Sattler, M.,Wilson, D.N.,Beckmann, R.
Structural Basis for Translational Stalling by Human Cytomegalovirus and Fungal Arginine Attenuator Peptide.
Mol.Cell, 40:138-, 2010

PubMed Abstract: Specific regulatory nascent chains establish direct interactions with the ribosomal tunnel, leading to translational stalling. Despite a wealth of biochemical data, structural insight into the mechanism of translational stalling in eukaryotes is still lacking. Here we use cryo-electron microscopy to visualize eukaryotic ribosomes stalled during the translation of two diverse regulatory peptides: the fungal arginine attenuator peptide (AAP) and the human cytomegalovirus (hCMV) gp48 upstream open reading frame 2 (uORF2). The C terminus of the AAP appears to be compacted adjacent to the peptidyl transferase center (PTC). Both nascent chains interact with ribosomal proteins L4 and L17 at tunnel constriction in a distinct fashion. Significant changes at the PTC were observed: the eukaryotic-specific loop of ribosomal protein L10e establishes direct contact with the CCA end of the peptidyl-tRNA (P-tRNA), which may be critical for silencing of the PTC during translational stalling. Our findings provide direct structural insight into two distinct eukaryotic stalling processes.

PubMed: 20932481
DOI: 10.1016/J.MOLCEL.2010.09.009

Experimental method

SOLUTION NMR