3er0: Difference between revisions

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'''Unreleased structure'''


The entry 3er0 is ON HOLD
==Crystal structure of the full length eIF5A from Saccharomyces cerevisiae==
<StructureSection load='3er0' size='340' side='right'caption='[[3er0]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3er0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ER0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ER0 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]] 3.35&#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=3er0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3er0 OCA], [https://pdbe.org/3er0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3er0 RCSB], [https://www.ebi.ac.uk/pdbsum/3er0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3er0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IF5A1_YEAST IF5A1_YEAST] mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Essential for polarized growth, a process necessary for G1/S transition. May mediate large range of effects of the polyamine spermidine in the cell.<ref>PMID:10229683</ref> <ref>PMID:16157662</ref> <ref>PMID:16408210</ref> <ref>PMID:16914118</ref> <ref>PMID:19338753</ref> <ref>PMID:19424157</ref> <ref>PMID:641056</ref> <ref>PMID:8307948</ref> <ref>PMID:9582285</ref>
== 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/er/3er0_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=3er0 ConSurf].
<div style="clear:both"></div>


Authors: Sanches, M., Dias, C.A.O., Aponi, L.H., Valentini, S.R., Guimaraes, B.
==See Also==
 
*[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]]
Description: Crystal structure of the full length eIF5A from Saccharomyces cerevisiae
== References ==
 
<references/>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 15 14:06:30 2008''
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Aponi LH]]
[[Category: Dias CAO]]
[[Category: Guimaraes B]]
[[Category: Sanches M]]
[[Category: Valentini SR]]

Latest revision as of 09:31, 6 September 2023

Crystal structure of the full length eIF5A from Saccharomyces cerevisiaeCrystal structure of the full length eIF5A from Saccharomyces cerevisiae

Structural highlights

3er0 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.35Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IF5A1_YEAST mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Essential for polarized growth, a process necessary for G1/S transition. May mediate large range of effects of the polyamine spermidine in the cell.[1] [2] [3] [4] [5] [6] [7] [8] [9]

Evolutionary Conservation

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

See Also

References

  1. ↑ Lee YB, Joe YA, Wolff EC, Dimitriadis EK, Park MH. Complex formation between deoxyhypusine synthase and its protein substrate, the eukaryotic translation initiation factor 5A (eIF5A) precursor. Biochem J. 1999 May 15;340 ( Pt 1):273-81. PMID:10229683
  2. ↑ Zanelli CF, Valentini SR. Pkc1 acts through Zds1 and Gic1 to suppress growth and cell polarity defects of a yeast eIF5A mutant. Genetics. 2005 Dec;171(4):1571-81. Epub 2005 Sep 12. PMID:16157662 doi:http://dx.doi.org/genetics.105.048082
  3. ↑ Chatterjee I, Gross SR, Kinzy TG, Chen KY. Rapid depletion of mutant eukaryotic initiation factor 5A at restrictive temperature reveals connections to actin cytoskeleton and cell cycle progression. Mol Genet Genomics. 2006 Mar;275(3):264-76. Epub 2006 Jan 12. PMID:16408210 doi:http://dx.doi.org/10.1007/s00438-005-0086-4
  4. ↑ Zanelli CF, Maragno AL, Gregio AP, Komili S, Pandolfi JR, Mestriner CA, Lustri WR, Valentini SR. eIF5A binds to translational machinery components and affects translation in yeast. Biochem Biophys Res Commun. 2006 Oct 6;348(4):1358-66. Epub 2006 Aug 7. PMID:16914118 doi:http://dx.doi.org/10.1016/j.bbrc.2006.07.195
  5. ↑ Gregio AP, Cano VP, Avaca JS, Valentini SR, Zanelli CF. eIF5A has a function in the elongation step of translation in yeast. Biochem Biophys Res Commun. 2009 Mar 20;380(4):785-90. Epub 2009 Jan 29. PMID:19338753 doi:http://dx.doi.org/S0006-291X(09)00203-4
  6. ↑ Saini P, Eyler DE, Green R, Dever TE. Hypusine-containing protein eIF5A promotes translation elongation. Nature. 2009 May 7;459(7243):118-21. PMID:19424157 doi:http://dx.doi.org/nature08034
  7. ↑ Benne R, Hershey JW. The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes. J Biol Chem. 1978 May 10;253(9):3078-87. PMID:641056
  8. ↑ Kang HA, Hershey JW. Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae. J Biol Chem. 1994 Feb 11;269(6):3934-40. PMID:8307948
  9. ↑ Zuk D, Jacobson A. A single amino acid substitution in yeast eIF-5A results in mRNA stabilization. EMBO J. 1998 May 15;17(10):2914-25. PMID:9582285 doi:http://dx.doi.org/10.1093/emboj/17.10.2914

3er0, resolution 3.35Å

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