1x18

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(New page: 200px<br /><applet load="1x18" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x18" /> '''Contact sites of ERA GTPase on the THERMUS T...)
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[[Image:1x18.gif|left|200px]]<br /><applet load="1x18" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1x18.gif|left|200px]]<br /><applet load="1x18" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1x18" />
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'''Contact sites of ERA GTPase on the THERMUS THERMOPHILUS 30S SUBUNIT'''<br />
'''Contact sites of ERA GTPase on the THERMUS THERMOPHILUS 30S SUBUNIT'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1X18 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X18 OCA].
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1X18 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X18 OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Agrawal, R.K.]]
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[[Category: Agrawal, R K.]]
[[Category: Barat, C.]]
[[Category: Barat, C.]]
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[[Category: Sharma, M.R.]]
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[[Category: Sharma, M R.]]
[[Category: contact sites of era protein on the 30s ribosomal subunit]]
[[Category: contact sites of era protein on the 30s ribosomal subunit]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:47:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:50:03 2008''

Revision as of 13:50, 21 February 2008


1x18

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Contact sites of ERA GTPase on 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

1X18 is a Protein complex structure of sequences 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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