| Structural highlights
1x1l is a 2 chain structure with sequence from Escherichia coli and Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Related: | 1fjf, 1ega, 1wf3, 1x18 |
| Resources: | FirstGlance, OCA, RCSB, PDBsum, TOPSAN |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Interaction of Era with the 30S ribosomal subunit implications for 30S subunit assembly.,Sharma MR, Barat C, Wilson DN, Booth TM, Kawazoe M, Hori-Takemoto C, Shirouzu M, Yokoyama S, Fucini P, Agrawal RK Mol Cell. 2005 Apr 29;18(3):319-29. PMID:15866174[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sharma MR, Barat C, Wilson DN, Booth TM, Kawazoe M, Hori-Takemoto C, Shirouzu M, Yokoyama S, Fucini P, Agrawal RK. Interaction of Era with the 30S ribosomal subunit implications for 30S subunit assembly. Mol Cell. 2005 Apr 29;18(3):319-29. PMID:15866174 doi:10.1016/j.molcel.2005.03.028
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