1x1l
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(New page: 200px<br /><applet load="1x1l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x1l" /> '''Interaction of ERA,a GTPase protein, with th...)
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Revision as of 03:40, 21 November 2007
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Interaction of ERA,a GTPase protein, with the 3'minor domain of the 16S rRNA within the THERMUS THERMOPHILUS 30S subunit.
Overview
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.
About this Structure
1X1L is a Single protein structure of sequence from Escherichia coli and Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
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
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