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8WI8

Cryo- EM structure of Mycobacterium smegmatis 50S ribosomal subunit (body 1) of 70S ribosome, bS1 and RafH.

Summary for 8WI8
Entry DOI10.2210/pdb8wi8/pdb
EMDB information37560
Descriptor50S ribosomal protein L2, 50S ribosomal protein L17, 50S ribosomal protein L18, ... (28 entities in total)
Functional Keywordsribosome, protein synthesis, mycobacterium smegmatis, hibernation promotion factor, hpf, rafh, hypoxia stress, cryo- em, single particle reconstruction
Biological sourceMycolicibacterium smegmatis MC2 155
More
Total number of polymer chains28
Total formula weight1406690.53
Authors
Kumar, N.,Sharma, S.,Kaushal, P.S. (deposition date: 2023-09-24, release date: 2024-02-28)
Primary citationKumar, N.,Sharma, S.,Kaushal, P.S.
Cryo- EM structure of the mycobacterial 70S ribosome in complex with ribosome hibernation promotion factor RafH.
Nat Commun, 15:638-638, 2024
Cited by
PubMed Abstract: Ribosome hibernation is a key survival strategy bacteria adopt under environmental stress, where a protein, hibernation promotion factor (HPF), transitorily inactivates the ribosome. Mycobacterium tuberculosis encounters hypoxia (low oxygen) as a major stress in the host macrophages, and upregulates the expression of RafH protein, which is crucial for its survival. The RafH, a dual domain HPF, an orthologue of bacterial long HPF (HPF), hibernates ribosome in 70S monosome form, whereas in other bacteria, the HPF induces 70S ribosome dimerization and hibernates its ribosome in 100S disome form. Here, we report the cryo- EM structure of M. smegmatis, a close homolog of M. tuberculosis, 70S ribosome in complex with the RafH factor at an overall 2.8 Å resolution. The N- terminus domain (NTD) of RafH binds to the decoding center, similarly to HPF NTD. In contrast, the C- terminus domain (CTD) of RafH, which is larger than the HPF CTD, binds to a distinct site at the platform binding center of the ribosomal small subunit. The two domain-connecting linker regions, which remain mostly disordered in earlier reported HPF structures, interact mainly with the anti-Shine Dalgarno sequence of the 16S rRNA.
PubMed: 38245551
DOI: 10.1038/s41467-024-44879-y
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.7 Å)
Structure validation

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數據於2024-11-13公開中

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