1efg: Difference between revisions

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{{Seed}}
[[Image:1efg.png|left|200px]]


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==THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTION==
The line below this paragraph, containing "STRUCTURE_1efg", creates the "Structure Box" on the page.
<StructureSection load='1efg' size='340' side='right'caption='[[1efg]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1efg]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EFG FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
{{STRUCTURE_1efg| PDB=1efg |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1efg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efg OCA], [https://pdbe.org/1efg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1efg RCSB], [https://www.ebi.ac.uk/pdbsum/1efg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1efg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EFG_THET8 EFG_THET8] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
== 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/ef/1efg_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=1efg ConSurf].
<div style="clear:both"></div>


===THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTION===
==See Also==
 
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
 
__TOC__
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</StructureSection>
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[[Category: Large Structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 8070396 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8070396}}
 
==About this Structure==
1EFG is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFG OCA].
 
==Reference==
<ref group="xtra">PMID:8070396</ref><references group="xtra"/>
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Czworkowski, J.]]
[[Category: Czworkowski J]]
[[Category: Moore, P B.]]
[[Category: Moore PB]]
[[Category: Steitz, T A.]]
[[Category: Steitz TA]]
[[Category: Wang, J.]]
[[Category: Wang J]]
[[Category: Elongation factor]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 25 11:11:48 2009''

Latest revision as of 10:01, 7 February 2024

THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTIONTHE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTION

Structural highlights

1efg is a 3 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EFG_THET8 Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.

Evolutionary Conservation

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

See Also

1efg, resolution 2.70Å

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