5ZZM
E. coli 50S subunit bound HflX protein in presence of ATP (AMP-PNP) and GTP (GMP-PNP) analogs.
Summary for 5ZZM
| Entry DOI | 10.2210/pdb5zzm/pdb |
| Related | 5ADY |
| EMDB information | 6979 |
| Descriptor | GTPase HflX, 5S rRNA, 23S rRNA (3 entities in total) |
| Functional Keywords | atpase, rna helicase, heat stress, ribosome |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 3 |
| Total formula weight | 1028489.27 |
| Authors | |
| Primary citation | Dey, S.,Biswas, C.,Sengupta, J. The universally conserved GTPase HflX is an RNA helicase that restores heat-damagedEscherichia coliribosomes. J. Cell Biol., 217:2519-2529, 2018 Cited by PubMed Abstract: The ribosome-associated GTPase HflX acts as an antiassociation factor upon binding to the 50S ribosomal subunit during heat stress in Although HflX is recognized as a guanosine triphosphatase, several studies have shown that the N-terminal domain 1 of HflX is capable of hydrolyzing adenosine triphosphate (ATP), but the functional role of its adenosine triphosphatase (ATPase) activity remains unknown. We demonstrate that HflX possesses ATP-dependent RNA helicase activity and is capable of unwinding large subunit ribosomal RNA. A cryo-electron microscopy structure of the 50S-HflX complex in the presence of nonhydrolyzable analogues of ATP and guanosine triphosphate hints at a mode of action for the RNA helicase and suggests the linker helical domain may have a determinant role in RNA unwinding. Heat stress results in inactivation of the ribosome, and we show that HflX can restore heat-damaged ribosomes and improve cell survival. PubMed: 29930203DOI: 10.1083/jcb.201711131 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (8.1 Å) |
Structure validation
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