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[[Image:1n0v.gif|left|200px]]<br /><applet load="1n0v" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1n0v, resolution 2.85&Aring;" />
'''Crystal structure of elongation factor 2'''<br />


==Overview==
==Crystal structure of elongation factor 2==
Two crystal structures of yeast translation elongation factor 2 (eEF2) were determined: the apo form at 2.9 A resolution and eEF2 in the presence of the translocation inhibitor sordarin at 2.1 A resolution. The overall conformation of apo eEF2 is similar to that of its prokaryotic homolog elongation factor G (EF-G) in complex with GDP. Upon sordarin binding, the three tRNA-mimicking C-terminal domains undergo substantial conformational changes, while the three N-terminal domains containing the nucleotide-binding site form an almost rigid unit. The conformation of eEF2 in complex with sordarin is entirely different from known conformations observed in crystal structures of EF-G or from cryo-EM studies of EF-G-70S complexes. The domain rearrangements induced by sordarin binding and the highly ordered drug-binding site observed in the eEF2-sordarin structure provide a high-resolution structural basis for the mechanism of sordarin inhibition. The two structures also emphasize the dynamic nature of the ribosomal translocase.
<StructureSection load='1n0v' size='340' side='right'caption='[[1n0v]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1n0v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The September 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Elongation Factors''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_9 10.2210/rcsb_pdb/mom_2006_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N0V FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</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=1n0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n0v OCA], [https://pdbe.org/1n0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n0v RCSB], [https://www.ebi.ac.uk/pdbsum/1n0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n0v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EF2_YEAST EF2_YEAST]
== 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/n0/1n0v_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=1n0v ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1N0V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The following page contains interesting information on the relation of 1N0V with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb81_1.html Elongation Factors]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N0V OCA].
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase., Jorgensen R, Ortiz PA, Carr-Schmid A, Nissen P, Kinzy TG, Andersen GR, Nat Struct Biol. 2003 May;10(5):379-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12692531 12692531]
[[Category: Elongation Factors]]
[[Category: Elongation Factors]]
[[Category: Large Structures]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Andersen GR]]
[[Category: Andersen, G R.]]
[[Category: Carr-Schmid A]]
[[Category: Carr-Schmid, A.]]
[[Category: Joergensen R]]
[[Category: Joergensen, R.]]
[[Category: Kinzy TG]]
[[Category: Kinzy, T G.]]
[[Category: Nissen P]]
[[Category: Nissen, P.]]
[[Category: Ortiz PA]]
[[Category: Ortiz, P A.]]
[[Category: g-protein cis-proline]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:01 2008''

Latest revision as of 10:51, 14 February 2024

Crystal structure of elongation factor 2Crystal structure of elongation factor 2

Structural highlights

1n0v is a 2 chain structure with sequence from Saccharomyces cerevisiae. The September 2006 RCSB PDB Molecule of the Month feature on Elongation Factors by David S. Goodsell is 10.2210/rcsb_pdb/mom_2006_9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.85Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EF2_YEAST

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1n0v, resolution 2.85Å

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