2YKR
30S ribosomal subunit with RsgA bound in the presence of GMPPNP
Summary for 2YKR
Entry DOI | 10.2210/pdb2ykr/pdb |
Related | 2VHP |
EMDB information | 1884 |
Descriptor | 16S RRNA, 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (22 entities in total) |
Functional Keywords | ribosome-hydrolase complex, ribosome biogenesis, yjeq, circularly permutated gtpase, ribosome/hydrolase |
Biological source | ESCHERICHIA COLI More |
Cellular location | Cytoplasm : E3PE32 |
Total number of polymer chains | 22 |
Total formula weight | 800897.55 |
Authors | |
Primary citation | Guo, Q.,Yuan, Y.,Xu, Y.,Feng, B.,Liu, L.,Chen, K.,Sun, M.,Yang, Z.,Lei, J.,Gao, N. Structural Basis for the Function of a Small Gtpase Rsga on the 30S Ribosomal Subunit Maturation Revealed by Cryoelectron Microscopy. Proc.Natl.Acad.Sci.USA, 108:13100-, 2011 Cited by PubMed Abstract: The bacterial RsgA, a circularly permutated GTPase, whose GTPase activity is dependent on the 30S ribosomal subunit, is a late-stage ribosome biogenesis factor involved in the 30S subunit maturation. The role of RsgA is to release another 30S biogenesis factor, RbfA, from the mature 30S subunit in a GTP-dependent manner. Using cryoelectron microscopy, we have determined the structure of the 30S subunit bound with RsgA in the presence of GMPPNP at subnanometer resolution. In the structure, RsgA binds to the central part of the 30S subunit, close to the decoding center, in a position that is incompatible with multiple biogenesis factors, all three translation initiation factors, as well as A-, P-site tRNAs and the 50S subunit. Further structural analysis not only provides a structural model for the RsgA-dependent release of RbfA from the nascent 30S subunit, but also indicates RsgA's role in the ribosomal protein assembly, to promote some tertiary binding protein incorporation. Moreover, together with available biochemical and genetic data, our results suggest that RsgA might be a general checkpoint protein in the late stage of the 30S subunit biogenesis, whose function is not only to release biogenesis factors (e.g., RbfA) from the nascent 30S subunit, but also to block the association of initiation factors to the premature 30S subunit. PubMed: 21788480DOI: 10.1073/PNAS.1104645108 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (9.8 Å) |
Structure validation
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