1cqu: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1cqu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cqu" /> '''SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN ...
 
OCA (talk | contribs)
No edit summary
 
(19 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1cqu.gif|left|200px]]<br /><applet load="1cqu" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1cqu" />
'''SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9'''<br />


==Overview==
==SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9==
The N-terminal domain of the ribosomal protein L9 forms a split, betaalphabeta structure with a long C-terminal helix. The folding, transitions of a 56 residue version of this protein have previously been, characterized, here we report the results of a study of a truncation, mutant corresponding to residues 1-51. The 51 residue protein adopts the, same fold as the 56 residue protein as judged by CD and two-dimensional, NMR, but it is less stable as judged by chemical and thermal denaturation, experiments. Studies with synthetic peptides demonstrate that the, C-terminal helix of the 51 residue version has very little propensity to, fold in isolation in contrast to the C-terminal helix of the 56 residue, variant. The folding rates of the two proteins, as measured by, stopped-flow fluorescence, are essentially identical, indicating that, formation of local structure in the C-terminal helix is not involved in, the rate-limiting step of folding.
<StructureSection load='1cqu' size='340' side='right'caption='[[1cqu]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cqu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CQU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cqu OCA], [https://pdbe.org/1cqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cqu RCSB], [https://www.ebi.ac.uk/pdbsum/1cqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cqu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RL9_GEOSE RL9_GEOSE] Binds to the 23S rRNA.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cq/1cqu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cqu ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The N-terminal domain of the ribosomal protein L9 forms a split betaalphabeta structure with a long C-terminal helix. The folding transitions of a 56 residue version of this protein have previously been characterized, here we report the results of a study of a truncation mutant corresponding to residues 1-51. The 51 residue protein adopts the same fold as the 56 residue protein as judged by CD and two-dimensional NMR, but it is less stable as judged by chemical and thermal denaturation experiments. Studies with synthetic peptides demonstrate that the C-terminal helix of the 51 residue version has very little propensity to fold in isolation in contrast to the C-terminal helix of the 56 residue variant. The folding rates of the two proteins, as measured by stopped-flow fluorescence, are essentially identical, indicating that formation of local structure in the C-terminal helix is not involved in the rate-limiting step of folding.


==About this Structure==
Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9.,Luisi DL, Kuhlman B, Sideras K, Evans PA, Raleigh DP J Mol Biol. 1999 May 28;289(1):167-74. PMID:10339414<ref>PMID:10339414</ref>
1CQU 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=1CQU OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9., Luisi DL, Kuhlman B, Sideras K, Evans PA, Raleigh DP, J Mol Biol. 1999 May 28;289(1):167-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10339414 10339414]
</div>
<div class="pdbe-citations 1cqu" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Ribosomal protein L9|Ribosomal protein L9]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hoffman, D.]]
[[Category: Hoffman D]]
[[Category: Hua, Y.]]
[[Category: Hua Y]]
[[Category: Kuhlman, B.]]
[[Category: Kuhlman B]]
[[Category: Raleigh, D.P.]]
[[Category: Raleigh DP]]
[[Category: nmr]]
[[Category: protein l9]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:41:06 2007''

Latest revision as of 08:22, 22 May 2024

SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA