1dv4

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(New page: 200px<br /><applet load="1dv4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dv4, resolution 4.50&Aring;" /> '''PARTIAL STRUCTURE OF...)
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[[Image:1dv4.jpg|left|200px]]<br /><applet load="1dv4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1dv4, resolution 4.50&Aring;" />
caption="1dv4, resolution 4.50&Aring;" />
'''PARTIAL STRUCTURE OF 16S RNA OF THE SMALL RIBOSOMAL SUBUNIT FROM THERMUS THERMOPHILUS'''<br />
'''PARTIAL STRUCTURE OF 16S RNA OF THE SMALL RIBOSOMAL SUBUNIT FROM THERMUS THERMOPHILUS'''<br />
==Overview==
==Overview==
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The electron density map of the small ribosomal subunit from Thermus, thermophilus, constructed at 4.5 A resolution, shows the recognizable, morphology of this particle, as well as structural features that were, interpreted as ribosomal RNA and proteins. Unbiased assignments, carried, out by quantitative covalent binding of heavy atom compounds at, predetermined sites, led to the localization of the surface of the, ribosomal protein S13 at a position compatible with previous assignments, whereas the surface of S11 was localized at a distance of about twice its, diameter from the site suggested for its center by neutron scattering., Proteins S5 and S7, whose structures have been determined, crystallographically, were visually placed in the map with no alterations, in their conformations. Regions suitable to host the fold of protein S15, were detected in several positions, all at a significant distance from the, location of this protein in the neutron scattering map. Targeting the 16S, RNA region, where mRNA docks to allow the formation of the initiation, complex by a mercurated mRNA analog, led to the characterization of its, vicinity.
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The electron density map of the small ribosomal subunit from Thermus thermophilus, constructed at 4.5 A resolution, shows the recognizable morphology of this particle, as well as structural features that were interpreted as ribosomal RNA and proteins. Unbiased assignments, carried out by quantitative covalent binding of heavy atom compounds at predetermined sites, led to the localization of the surface of the ribosomal protein S13 at a position compatible with previous assignments, whereas the surface of S11 was localized at a distance of about twice its diameter from the site suggested for its center by neutron scattering. Proteins S5 and S7, whose structures have been determined crystallographically, were visually placed in the map with no alterations in their conformations. Regions suitable to host the fold of protein S15 were detected in several positions, all at a significant distance from the location of this protein in the neutron scattering map. Targeting the 16S RNA region, where mRNA docks to allow the formation of the initiation complex by a mercurated mRNA analog, led to the characterization of its vicinity.
==About this Structure==
==About this Structure==
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1DV4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with WO2 as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1C59. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DV4 OCA].
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1DV4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=WO2:'>WO2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1C59. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DV4 OCA].
==Reference==
==Reference==
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[[Category: thermus thermophilus]]
[[Category: thermus thermophilus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:36:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:48 2008''

Revision as of 10:20, 21 February 2008


1dv4, resolution 4.50Å

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PARTIAL STRUCTURE OF 16S RNA OF THE SMALL RIBOSOMAL SUBUNIT FROM THERMUS THERMOPHILUS

Overview

The electron density map of the small ribosomal subunit from Thermus thermophilus, constructed at 4.5 A resolution, shows the recognizable morphology of this particle, as well as structural features that were interpreted as ribosomal RNA and proteins. Unbiased assignments, carried out by quantitative covalent binding of heavy atom compounds at predetermined sites, led to the localization of the surface of the ribosomal protein S13 at a position compatible with previous assignments, whereas the surface of S11 was localized at a distance of about twice its diameter from the site suggested for its center by neutron scattering. Proteins S5 and S7, whose structures have been determined crystallographically, were visually placed in the map with no alterations in their conformations. Regions suitable to host the fold of protein S15 were detected in several positions, all at a significant distance from the location of this protein in the neutron scattering map. Targeting the 16S RNA region, where mRNA docks to allow the formation of the initiation complex by a mercurated mRNA analog, led to the characterization of its vicinity.

About this Structure

1DV4 is a Protein complex structure of sequences from Geobacillus stearothermophilus and Thermus thermophilus with as ligand. This structure supersedes the now removed PDB entry 1C59. Full crystallographic information is available from OCA.

Reference

The small ribosomal subunit from Thermus thermophilus at 4.5 A resolution: pattern fittings and the identification of a functional site., Tocilj A, Schlunzen F, Janell D, Gluhmann M, Hansen HA, Harms J, Bashan A, Bartels H, Agmon I, Franceschi F, Yonath A, Proc Natl Acad Sci U S A. 1999 Dec 7;96(25):14252-7. PMID:10588692

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