5ADY

Cryo-EM structures of the 50S ribosome subunit bound with HflX

Summary for 5ADY

• Entry DOI: 10.2210/pdb5ady/pdb
• Related: 1B75 1D6K 1DFU 2J28 2VRH 487D 4CSU 4UY8 5AKA
• EMDB information: 3133
• Descriptor: 50S RIBOSOMAL PROTEIN L32, 23S RRNA, 50S RIBOSOMAL PROTEIN L2, ... (36 entities in total)
• Functional Keywords: ribosome, ribosome rescue
• Biological source: ESCHERICHIA COLI K-12; More
• Total number of polymer chains: 34
• Total formula weight: 1448692.51

Authors

Zhang, Y.,Mandava, C.S.,Cao, W.,Li, X.,Zhang, D.,Li, N.,Zhang, Y.,Zhang, X.,Qin, Y.,Mi, K.,Lei, J.,Sanyal, S.,Gao, N. (deposition date: 2015-08-25, release date: 2015-10-14, Last modification date: 2024-05-08)

Primary citation

Zhang, Y.,Mandava, C.S.,Cao, W.,Li, X.,Zhang, D.,Li, N.,Zhang, Y.,Zhang, X.,Qin, Y.,Mi, K.,Lei, J.,Sanyal, S.,Gao, N.
Hflx is a Ribosome Splitting Factor Rescuing Stalled Ribosomes Under Stress Conditions
Nat.Struct.Mol.Biol., 22:906-, 2015

PubMed Abstract: Adverse cellular conditions often lead to nonproductive translational stalling and arrest of ribosomes on mRNAs. Here, we used fast kinetics and cryo-EM to characterize Escherichia coli HflX, a GTPase with unknown function. Our data reveal that HflX is a heat shock-induced ribosome-splitting factor capable of dissociating vacant as well as mRNA-associated ribosomes with deacylated tRNA in the peptidyl site. Structural data demonstrate that the N-terminal effector domain of HflX binds to the peptidyl transferase center in a strikingly similar manner as that of the class I release factors and induces dramatic conformational changes in central intersubunit bridges, thus promoting subunit dissociation. Accordingly, loss of HflX results in an increase in stalled ribosomes upon heat shock. These results suggest a primary role of HflX in rescuing translationally arrested ribosomes under stress conditions.

PubMed: 26458047
DOI: 10.1038/NSMB.3103

Experimental method

ELECTRON MICROSCOPY (4.5 Å)