1aip: Difference between revisions

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New page: left|200px<br /><applet load="1aip" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aip, resolution 3.0Å" /> '''EF-TU EF-TS COMPLEX F...
 
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[[Image:1aip.gif|left|200px]]<br /><applet load="1aip" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1aip, resolution 3.0&Aring;" />
'''EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS'''<br />


==Overview==
==EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS==
In order to study nucleotide exchange mechanisms in GTP-binding proteins, we have determined the crystal structure of the complex formed by the, elongation factor Tu (EF-Tu) and its exchange factor Ts (EF-Ts) from, Thermus thermophilus. The complex is a dyad symmetrical heterotetramer in, which each EF-Tu, through a bipartite interface, interacts with two, subunits of EF-Ts, explaining the need for a dimeric exchange factor. The, architecture of the assembly is distinctly different from that of the, corresponding heterodimeric E. coli complex, in which the monomeric E., coli EF-Ts remarkably forms essentially the same bipartite interface with, EF-Tu through a sequence/structural repeat. GDP is released primarily by a, Ts-induced peptide flip in the nucleotide binding pocket that disrupts, hydrogen bonds to the phosphates and repositions the peptide carbonyl so, as to sterically and electrostatically eject the GDP. The exchange, mechanism may have useful implications for receptor-induced exchange in, heterotrimeric G proteins.
<StructureSection load='1aip' size='340' side='right'caption='[[1aip]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1aip]] is a 8 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=1AIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AIP 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]] 3&#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=1aip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aip OCA], [https://pdbe.org/1aip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aip RCSB], [https://www.ebi.ac.uk/pdbsum/1aip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aip ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EFTU1_THETH EFTU1_THETH] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
== 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/ai/1aip_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=1aip ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1AIP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AIP OCA].
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus., Wang Y, Jiang Y, Meyering-Voss M, Sprinzl M, Sigler PB, Nat Struct Biol. 1997 Aug;4(8):650-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9253415 9253415]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Jiang, Y.]]
[[Category: Jiang Y]]
[[Category: Meyering-Voss, M.]]
[[Category: Meyering-Voss M]]
[[Category: Sigler, P.B.]]
[[Category: Sigler PB]]
[[Category: Sprinzl, M.]]
[[Category: Sprinzl M]]
[[Category: Wang, Y.]]
[[Category: Wang Y]]
[[Category: complex of two elongation factors]]
[[Category: elongation factor]]
[[Category: gtp-binding]]
[[Category: nucleotide exchange]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:53:08 2007''

Latest revision as of 18:25, 13 March 2024

EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUSEF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS

Structural highlights

1aip is a 8 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 3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EFTU1_THETH This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.

Evolutionary Conservation

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

See Also

1aip, resolution 3.00Å

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