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7PWO

Cryo-EM structure of Giardia lamblia ribosome at 2.75 A resolution

This is a non-PDB format compatible entry.
Summary for 7PWO
Entry DOI10.2210/pdb7pwo/pdb
EMDB information13683
DescriptorRibosomal protein S19e, Ribosomal protein S27, 40S ribosomal protein S26, ... (76 entities in total)
Functional Keywordsribosome, giardia, parasite
Biological sourceGiardia lamblia ATCC 50803
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Total number of polymer chains74
Total formula weight2699463.80
Authors
Hiregange, D.G.,Rivalta, A.,Bose, T.,Breiner-Goldstein, E.,Samiya, S.,Cimicata, G.,Kulakova, L.,Zimmerman, E.,Bashan, A.,Herzberg, O.,Yonath, A. (deposition date: 2021-10-07, release date: 2022-04-20, Last modification date: 2024-11-13)
Primary citationHiregange, D.G.,Rivalta, A.,Bose, T.,Breiner-Goldstein, E.,Samiya, S.,Cimicata, G.,Kulakova, L.,Zimmerman, E.,Bashan, A.,Herzberg, O.,Yonath, A.
Cryo-EM structure of the ancient eukaryotic ribosome from the human parasite Giardia lamblia.
Nucleic Acids Res., 50:1770-1782, 2022
Cited by
PubMed Abstract: Giardiasis is a disease caused by the protist Giardia lamblia. As no human vaccines have been approved so far against it, and resistance to current drugs is spreading, new strategies for combating giardiasis need to be developed. The G. lamblia ribosome may provide a promising therapeutic target due to its distinct sequence differences from ribosomes of most eukaryotes and prokaryotes. Here, we report the cryo-electron microscopy structure of the G. lamblia (WB strain) ribosome determined at 2.75 Å resolution. The ribosomal RNA is the shortest known among eukaryotes, and lacks nearly all the eukaryote-specific ribosomal RNA expansion segments. In contrast, the ribosomal proteins are typically eukaryotic with some species-specific insertions/extensions. Most typical inter-subunit bridges are maintained except for one missing contact site. Unique structural features are located mainly at the ribosome's periphery. These may be exploited as target sites for the design of new compounds that inhibit selectively the parasite's ribosomal activity.
PubMed: 35100413
DOI: 10.1093/nar/gkac046
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.75 Å)
Structure validation

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