1nkw: Difference between revisions
New page: left|200px<br /><applet load="1nkw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nkw, resolution 3.10Å" /> '''Crystal Structure Of... |
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[[Image:1nkw.gif|left|200px]]<br /><applet load="1nkw" size=" | [[Image:1nkw.gif|left|200px]]<br /><applet load="1nkw" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1nkw, resolution 3.10Å" /> | caption="1nkw, resolution 3.10Å" /> | ||
'''Crystal Structure Of The Large Ribosomal Subunit From Deinococcus Radiodurans'''<br /> | '''Crystal Structure Of The Large Ribosomal Subunit From Deinococcus Radiodurans'''<br /> | ||
==Overview== | ==Overview== | ||
We describe the high resolution structure of the large ribosomal subunit | We describe the high resolution structure of the large ribosomal subunit from Deinococcus radiodurans (D50S), a gram-positive mesophile suitable for binding of antibiotics and functionally relevant ligands. The over-all structure of D50S is similar to that from the archae bacterium Haloarcula marismortui (H50S); however, a detailed comparison revealed significant differences, for example, in the orientation of nucleotides in peptidyl transferase center and in the structures of many ribosomal proteins. Analysis of ribosomal features involved in dynamic aspects of protein biosynthesis that are partially or fully disordered in H50S revealed the conformations of intersubunit bridges in unbound subunits, suggesting how they may change upon subunit association and how movements of the L1-stalk may facilitate the exit of tRNA. | ||
==About this Structure== | ==About this Structure== | ||
1NKW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. This structure | 1NKW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. This structure supersedes the now removed PDB entries 1LNR, 1KPJ and 1KC9. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NKW OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Franceschi, F.]] | [[Category: Franceschi, F.]] | ||
[[Category: Gat, S.]] | [[Category: Gat, S.]] | ||
[[Category: Harms, J | [[Category: Harms, J M.]] | ||
[[Category: Schluenzen, F.]] | [[Category: Schluenzen, F.]] | ||
[[Category: Yonath, A.]] | [[Category: Yonath, A.]] | ||
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[[Category: ribosome; large subunit; 50s; deinococcus radiodurans; x-ray structure; peptidyl-transferase]] | [[Category: ribosome; large subunit; 50s; deinococcus radiodurans; x-ray structure; peptidyl-transferase]] | ||
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Crystal Structure Of The Large Ribosomal Subunit From Deinococcus Radiodurans
OverviewOverview
We describe the high resolution structure of the large ribosomal subunit from Deinococcus radiodurans (D50S), a gram-positive mesophile suitable for binding of antibiotics and functionally relevant ligands. The over-all structure of D50S is similar to that from the archae bacterium Haloarcula marismortui (H50S); however, a detailed comparison revealed significant differences, for example, in the orientation of nucleotides in peptidyl transferase center and in the structures of many ribosomal proteins. Analysis of ribosomal features involved in dynamic aspects of protein biosynthesis that are partially or fully disordered in H50S revealed the conformations of intersubunit bridges in unbound subunits, suggesting how they may change upon subunit association and how movements of the L1-stalk may facilitate the exit of tRNA.
About this StructureAbout this Structure
1NKW is a Protein complex structure of sequences from Deinococcus radiodurans. This structure supersedes the now removed PDB entries 1LNR, 1KPJ and 1KC9. Full crystallographic information is available from OCA.
ReferenceReference
High resolution structure of the large ribosomal subunit from a mesophilic eubacterium., Harms J, Schluenzen F, Zarivach R, Bashan A, Gat S, Agmon I, Bartels H, Franceschi F, Yonath A, Cell. 2001 Nov 30;107(5):679-88. PMID:11733066
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