1efu: Difference between revisions

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New page: left|200px<br /> <applet load="1efu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1efu, resolution 2.5Å" /> '''ELONGATION FACTOR CO...
 
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[[Image:1efu.gif|left|200px]]<br />
<applet load="1efu" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1efu, resolution 2.5&Aring;" />
'''ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI'''<br />


==Overview==
==ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI==
The crystal structure of the EF-Tu.EF-Ts complex from Escherichia coli has, been determined to a resolution of 2.5 A. The complex contains two, subunits of each of the elongation factors. The two EF-Ts molecules form a, tight dimer, but there is little contact between the two EF-Tu molecules., The interaction of EF-Ts with EF-Tu results principally in the disruption, of the Mg2+ ion binding site, thereby reducing the affinity of EF-Tu for, guanine nucleotides.
<StructureSection load='1efu' size='340' side='right'caption='[[1efu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1efu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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=1EFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EFU 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]] 2.5&#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=1efu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efu OCA], [https://pdbe.org/1efu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1efu RCSB], [https://www.ebi.ac.uk/pdbsum/1efu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1efu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EFTU2_ECOLI EFTU2_ECOLI] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118]  May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118]
== 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/1efu_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=1efu ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1EFU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1EFU 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EFU OCA].
*[[Elongation factor|Elongation factor]]
 
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
==Reference==
__TOC__
The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution., Kawashima T, Berthet-Colominas C, Wulff M, Cusack S, Leberman R, Nature. 1996 Feb 8;379(6565):511-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8596629 8596629]
</StructureSection>
[[Category: Elongation Factors]]
[[Category: Elongation Factors]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Berthet-Colominas, C.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Cusack, S.]]
[[Category: Berthet-Colominas C]]
[[Category: Kawashima, T.]]
[[Category: Cusack S]]
[[Category: Leberman, R.]]
[[Category: Kawashima T]]
[[Category: Wulff, M.]]
[[Category: Leberman R]]
[[Category: complex (two elongation factors)]]
[[Category: Wulff M]]
[[Category: elongation factor]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 08:59:26 2007''

Latest revision as of 10:02, 7 February 2024

ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLIELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI

Structural highlights

1efu is a 4 chain structure with sequence from Escherichia coli. 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 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EFTU2_ECOLI This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118]

Evolutionary Conservation

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

See Also

1efu, resolution 2.50Å

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