1elo: Difference between revisions

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[[Image:1elo.gif|left|200px]]


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==ELONGATION FACTOR G WITHOUT NUCLEOTIDE==
The line below this paragraph, containing "STRUCTURE_1elo", creates the "Structure Box" on the page.
<StructureSection load='1elo' size='340' side='right'caption='[[1elo]], [[Resolution|resolution]] 2.80&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'>[[1elo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELO 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]] 2.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1elo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elo OCA], [https://pdbe.org/1elo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elo RCSB], [https://www.ebi.ac.uk/pdbsum/1elo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elo ProSAT]</span></td></tr>
{{STRUCTURE_1elo| PDB=1elo |  SCENE= }}
</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/el/1elo_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=1elo ConSurf].
<div style="clear:both"></div>


'''ELONGATION FACTOR G WITHOUT NUCLEOTIDE'''
==See Also==
 
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The crystal structure of Thermus thermophilus elongation factor G without guanine nucleotide was determined to 2.85 A. This GTPase has five domains with overall dimensions of 50 x 60 x 118 A. The GTP binding domain has a core common to other GTPases with a unique subdomain which probably functions as an intrinsic nucleotide exchange factor. Domains I and II are homologous to elongation factor Tu and their arrangement, both with and without GDP, is more similar to elongation factor Tu in complex with a GTP analogue than with GDP. Domains III and V show structural similarities to ribosomal proteins. Domain IV protrudes from the main body of the protein and has an extraordinary topology with a left-handed cross-over connection between two parallel beta-strands.
[[Category: Large Structures]]
 
[[Category: Thermus thermophilus HB8]]
==About this Structure==
[[Category: Aevarsson A]]
1ELO is a [[Single protein]] structure of sequence 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=1ELO OCA].
[[Category: Al-Karadaghi S]]
 
[[Category: Brazhnikov E]]
==Reference==
[[Category: Chirgadze Yu]]
Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus., AEvarsson A, Brazhnikov E, Garber M, Zheltonosova J, Chirgadze Y, al-Karadaghi S, Svensson LA, Liljas A, EMBO J. 1994 Aug 15;13(16):3669-77. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8070397 8070397]
[[Category: Garber M]]
[[Category: Single protein]]
[[Category: Liljas A]]
[[Category: Thermus thermophilus]]
[[Category: Svensson LA]]
[[Category: Aevarsson, A.]]
[[Category: Zheltonosova J]]
[[Category: Al-Karadaghi, S.]]
[[Category: Brazhnikov, E.]]
[[Category: Chirgadze, Yu.]]
[[Category: Garber, M.]]
[[Category: Liljas, A.]]
[[Category: Svensson, L A.]]
[[Category: Zheltonosova, J.]]
[[Category: Elongation factor]]
[[Category: Gtp binding protein]]
[[Category: Hydrolase]]
[[Category: Ribosomal translocase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:15:11 2008''

Latest revision as of 10:04, 7 February 2024

ELONGATION FACTOR G WITHOUT NUCLEOTIDEELONGATION FACTOR G WITHOUT NUCLEOTIDE

Structural highlights

1elo is a 1 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
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

1elo, resolution 2.80Å

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