1ovy: Difference between revisions

Revision as of 15:22, 21 February 2008

Solution Structure of Ribosomal Protein L18 from Bacillus stearothermophilus

OverviewOverview

A medium resolution solution structure has been obtained for L18 from Bacillus stearothermophilus (BstL18), a ribosomal protein that stabilizes the tertiary structure of 5S rRNA and mediates its interaction with the rest of the large subunit. The N-terminal 22 amino acid residues of BstL18 are unstructured in solution. Its remaining 98 residues form a globular domain that has the same topology as the globular domains of other L18s, but the orientation of helices is different. This conformational peculiarity should not prevent BstL18 from functioning in the ribosome the same way as other L18s.

About this StructureAbout this Structure

1OVY is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

ReferenceReference

The solution structure of ribosomal protein L18 from Bacillus stearothermophilus., Turner CF, Moore PB, J Mol Biol. 2004 Jan 16;335(3):679-84. PMID:14687565

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OCA

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 '''Solution Structure of Ribosomal Protein L18 from Bacillus stearothermophilus'''<br />
 ==Overview==
-A medium resolution solution structure has been obtained for L18 from, Bacillus stearothermophilus (BstL18), a ribosomal protein that stabilizes, the tertiary structure of 5S rRNA and mediates its interaction with the, rest of the large subunit. The N-terminal 22 amino acid residues of BstL18, are unstructured in solution. Its remaining 98 residues form a globular, domain that has the same topology as the globular domains of other L18s, but the orientation of helices is different. This conformational, peculiarity should not prevent BstL18 from functioning in the ribosome the, same way as other L18s.
+A medium resolution solution structure has been obtained for L18 from Bacillus stearothermophilus (BstL18), a ribosomal protein that stabilizes the tertiary structure of 5S rRNA and mediates its interaction with the rest of the large subunit. The N-terminal 22 amino acid residues of BstL18 are unstructured in solution. Its remaining 98 residues form a globular domain that has the same topology as the globular domains of other L18s, but the orientation of helices is different. This conformational peculiarity should not prevent BstL18 from functioning in the ribosome the same way as other L18s.
 ==About this Structure==
-OVY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OVY OCA].
+OVY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OVY OCA].
 ==Reference==
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 [[Category: Geobacillus stearothermophilus]]
 [[Category: Single protein]]
-[[Category: Moore, P.B.]]
+[[Category: Moore, P B.]]
-[[Category: Turner, C.F.]]
+[[Category: Turner, C F.]]
 [[Category: ribosomal protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:14:29 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:09 2008''