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New page: left|200px<br /><applet load="1d1n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d1n" /> '''SOLUTION STRUCTURE OF THE FMET-TRNAFMET BIND...
 
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[[Image:1d1n.gif|left|200px]]<br /><applet load="1d1n" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1d1n" />
'''SOLUTION STRUCTURE OF THE FMET-TRNAFMET BINDING DOMAIN OF BECILLUS STEAROTHERMOPHILLUS TRANSLATION INITIATION FACTOR IF2'''<br />


==Overview==
==SOLUTION STRUCTURE OF THE FMET-TRNAFMET BINDING DOMAIN OF BECILLUS STEAROTHERMOPHILLUS TRANSLATION INITIATION FACTOR IF2==
The three-dimensional structure of the fMet-tRNA(fMet) -binding domain of, translation initiation factor IF2 from Bacillus stearothermophilus has, been determined by heteronuclear NMR spectroscopy. Its structure consists, of six antiparallel beta-strands, connected via loops, and forms a closed, beta-barrel similar to domain II of elongation factors EF-Tu and EF-G, despite low sequence homology. Two structures of the ternary complexes of, the EF-Tu small middle dotaminoacyl-tRNA small middle dot GDP analogue, have been reported and were used to propose and discuss the possible, fMet-tRNA(fMet)-binding site of IF2.
<StructureSection load='1d1n' size='340' side='right'caption='[[1d1n]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1d1n]] 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=1D1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D1N 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=1d1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d1n OCA], [https://pdbe.org/1d1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d1n RCSB], [https://www.ebi.ac.uk/pdbsum/1d1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d1n ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IF2_GEOSE IF2_GEOSE] One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
== 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/d1/1d1n_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=1d1n ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of the fMet-tRNA(fMet) -binding domain of translation initiation factor IF2 from Bacillus stearothermophilus has been determined by heteronuclear NMR spectroscopy. Its structure consists of six antiparallel beta-strands, connected via loops, and forms a closed beta-barrel similar to domain II of elongation factors EF-Tu and EF-G, despite low sequence homology. Two structures of the ternary complexes of the EF-Tu small middle dotaminoacyl-tRNA small middle dot GDP analogue have been reported and were used to propose and discuss the possible fMet-tRNA(fMet)-binding site of IF2.


==About this Structure==
Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2.,Meunier S, Spurio R, Czisch M, Wechselberger R, Guenneugues M, Gualerzi CO, Boelens R EMBO J. 2000 Apr 17;19(8):1918-26. PMID:10775275<ref>PMID:10775275</ref>
1D1N 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=1D1N OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2., Meunier S, Spurio R, Czisch M, Wechselberger R, Guenneugues M, Gualerzi CO, Boelens R, EMBO J. 2000 Apr 17;19(8):1918-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10775275 10775275]
</div>
<div class="pdbe-citations 1d1n" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Czisch, M.]]
[[Category: Czisch M]]
[[Category: Gueunneugues, M.]]
[[Category: Gueunneugues M]]
[[Category: Meunier, S.]]
[[Category: Meunier S]]
[[Category: Spurio, S.]]
[[Category: Spurio S]]
[[Category: Wechselberger, R.]]
[[Category: Wechselberger R]]
[[Category: beta-barrel]]
 
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Latest revision as of 08:22, 22 May 2024

SOLUTION STRUCTURE OF THE FMET-TRNAFMET BINDING DOMAIN OF BECILLUS STEAROTHERMOPHILLUS TRANSLATION INITIATION FACTOR IF2

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