1g1x: Difference between revisions
New page: left|200px<br /><applet load="1g1x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g1x, resolution 2.6Å" /> '''STRUCTURE OF RIBOSOMA... |
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[[Image:1g1x.gif|left|200px]]<br /><applet load="1g1x" size=" | [[Image:1g1x.gif|left|200px]]<br /><applet load="1g1x" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1g1x, resolution 2.6Å" /> | caption="1g1x, resolution 2.6Å" /> | ||
'''STRUCTURE OF RIBOSOMAL PROTEINS S15, S6, S18, AND 16S RIBOSOMAL RNA'''<br /> | '''STRUCTURE OF RIBOSOMAL PROTEINS S15, S6, S18, AND 16S RIBOSOMAL RNA'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of a 70-kilodalton ribonucleoprotein complex from | The crystal structure of a 70-kilodalton ribonucleoprotein complex from the central domain of the Thermus thermophilus 30S ribosomal subunit was solved at 2.6 angstrom resolution. The complex consists of a 104-nucleotide RNA fragment composed of two three-helix junctions that lie at the end of a central helix, and the ribosomal proteins S15, S6, and S18. S15 binds the ribosomal RNA early in the assembly of the 30S ribosomal subunit, stabilizing a conformational reorganization of the two three-helix junctions that creates the RNA fold necessary for subsequent binding of S6 and S18. The structure of the complex demonstrates the central role of S15-induced reorganization of central domain RNA for the subsequent steps of ribosome assembly. | ||
==About this Structure== | ==About this Structure== | ||
1G1X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. This structure | 1G1X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. This structure supersedes the now removed PDB entry 1EKC. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1X OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Agalarov, S | [[Category: Agalarov, S C.]] | ||
[[Category: Funke, P | [[Category: Funke, P M.]] | ||
[[Category: Prasad, G | [[Category: Prasad, G S.]] | ||
[[Category: Stout, C | [[Category: Stout, C D.]] | ||
[[Category: Williamson, J | [[Category: Williamson, J R.]] | ||
[[Category: ribosomal proteins s15]] | [[Category: ribosomal proteins s15]] | ||
[[Category: ribosome]] | [[Category: ribosome]] | ||
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[[Category: s6]] | [[Category: s6]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:08 2008'' | ||
Revision as of 10:45, 21 February 2008
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STRUCTURE OF RIBOSOMAL PROTEINS S15, S6, S18, AND 16S RIBOSOMAL RNA
Overview
The crystal structure of a 70-kilodalton ribonucleoprotein complex from the central domain of the Thermus thermophilus 30S ribosomal subunit was solved at 2.6 angstrom resolution. The complex consists of a 104-nucleotide RNA fragment composed of two three-helix junctions that lie at the end of a central helix, and the ribosomal proteins S15, S6, and S18. S15 binds the ribosomal RNA early in the assembly of the 30S ribosomal subunit, stabilizing a conformational reorganization of the two three-helix junctions that creates the RNA fold necessary for subsequent binding of S6 and S18. The structure of the complex demonstrates the central role of S15-induced reorganization of central domain RNA for the subsequent steps of ribosome assembly.
About this Structure
1G1X is a Protein complex structure of sequences from Thermus thermophilus. This structure supersedes the now removed PDB entry 1EKC. Full crystallographic information is available from OCA.
Reference
Structure of the S15,S6,S18-rRNA complex: assembly of the 30S ribosome central domain., Agalarov SC, Sridhar Prasad G, Funke PM, Stout CD, Williamson JR, Science. 2000 Apr 7;288(5463):107-13. PMID:10753109
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