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New page: left|200px<br /><applet load="1rip" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rip" /> '''RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF T...
 
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[[Image:1rip.gif|left|200px]]<br /><applet load="1rip" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1rip" />
'''RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF THE THREE-DIMENSIONAL STRUCTURE BY 1H-AND 15N-NMR'''<br />


==Overview==
==RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF THE THREE-DIMENSIONAL STRUCTURE BY 1H-AND 15N-NMR==
The structure of ribosomal protein S17 from Bacillus stearothermophilus, was investigated by two-dimensional homonuclear and heteronuclear magnetic, resonance spectroscopy. The 1H and 15N chemical shift assignments are, largely complete, and a preliminary structural characterization is, presented. The protein consists of five beta-strands that form a single, antiparallel beta-sheet with Greek-key topology. The beta-strands are, connected by several extended loops, and two of these contain residue, types that are frequently seen in the RNA-binding sites of proteins., Additionally, two point mutations that affect antibiotic resistance, translational fidelity, and ribosome assembly are located in these two, regions of the protein. Since these potential RNA-binding sites are, distributed over a large surface of the protein, it appears that the, molecule may interact with several regions of 16S rRNA.
<StructureSection load='1rip' size='340' side='right'caption='[[1rip]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rip]] 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=1RIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RIP 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=1rip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rip OCA], [https://pdbe.org/1rip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rip RCSB], [https://www.ebi.ac.uk/pdbsum/1rip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rip ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RS17_GEOSE RS17_GEOSE] One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.[HAMAP-Rule:MF_01345]
== 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/ri/1rip_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=1rip ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of ribosomal protein S17 from Bacillus stearothermophilus was investigated by two-dimensional homonuclear and heteronuclear magnetic resonance spectroscopy. The 1H and 15N chemical shift assignments are largely complete, and a preliminary structural characterization is presented. The protein consists of five beta-strands that form a single antiparallel beta-sheet with Greek-key topology. The beta-strands are connected by several extended loops, and two of these contain residue types that are frequently seen in the RNA-binding sites of proteins. Additionally, two point mutations that affect antibiotic resistance, translational fidelity, and ribosome assembly are located in these two regions of the protein. Since these potential RNA-binding sites are distributed over a large surface of the protein, it appears that the molecule may interact with several regions of 16S rRNA.


==About this Structure==
Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.,Golden BL, Hoffman DW, Ramakrishnan V, White SW Biochemistry. 1993 Nov 30;32(47):12812-20. PMID:8251502<ref>PMID:8251502</ref>
1RIP 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=1RIP OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR., Golden BL, Hoffman DW, Ramakrishnan V, White SW, Biochemistry. 1993 Nov 30;32(47):12812-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8251502 8251502]
</div>
<div class="pdbe-citations 1rip" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Ribosomal protein S17|Ribosomal protein S17]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Golden, B.L.]]
[[Category: Golden BL]]
[[Category: Hoffman, D.W.]]
[[Category: Hoffman DW]]
[[Category: Ramakrishnan, V.]]
[[Category: Ramakrishnan V]]
[[Category: White, S.W.]]
[[Category: White SW]]
[[Category: ribosomal protein]]
 
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