1X1L

Interaction of ERA,a GTPase protein, with the 3'minor domain of the 16S rRNA within the THERMUS THERMOPHILUS 30S subunit.

Summary for 1X1L

• Entry DOI: 10.2210/pdb1x1l/pdb
• Related: 1EGA 1FJF 1WF3 1X18
• Descriptor: RNA (130-MER), GTP-binding protein era (2 entities in total)
• Functional Keywords: interaction of era protein with the 3'minor domain of 16s rrna, structural protein-rna complex, structural protein/rna
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 2
• Total formula weight: 76161.32

Authors

Sharma, M.R.,Barat, C.,Agrawal, R.K. (deposition date: 2005-04-06, release date: 2005-05-17, Last modification date: 2024-03-13)

Primary citation

Sharma, M.R.,Barat, C.,Wilson, D.N.,Booth, T.M.,Kawazoe, M.,Hori-Takemoto, C.,Shirouzu, M.,Yokoyama, S.,Fucini, P.,Agrawal, R.K.
Interaction of Era with the 30S Ribosomal Subunit Implications for 30S Subunit Assembly
Mol.Cell, 18:319-329, 2005

PubMed Abstract: Era (E. coliRas-like protein) is a highly conserved and essential GTPase in bacteria. It binds to the 16S ribosomal RNA (rRNA) of the small (30S) ribosomal subunit, and its depletion leads to accumulation of an unprocessed precursor of the 16S rRNA. We have obtained a three-dimensional cryo-electron microscopic map of the Thermus thermophilus 30S-Era complex. Era binds in the cleft between the head and platform of the 30S subunit and locks the subunit in a conformation that is not favorable for association with the large (50S) ribosomal subunit. The RNA binding KH motif present within the C-terminal domain of Era interacts with the conserved nucleotides in the 3' region of the 16S rRNA. Furthermore, Era makes contact with several assembly elements of the 30S subunit. These observations suggest a direct involvement of Era in the assembly and maturation of the 30S subunit.

PubMed: 15866174
DOI: 10.1016/j.molcel.2005.03.028

Experimental method

ELECTRON MICROSCOPY (13.5 Å)