1e20: Difference between revisions

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New page: left|200px<br /> <applet load="1e20" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e20, resolution 2.02Å" /> '''THE FMN BINDING PRO...
 
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[[Image:1e20.gif|left|200px]]<br />
<applet load="1e20" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1e20, resolution 2.02&Aring;" />
'''THE FMN BINDING PROTEIN ATHAL3'''<br />


==Overview==
==The FMN binding protein AtHal3==
BACKGROUND: The Arabidopsis thaliana HAL3 gene product encodes for an, FMN-binding protein (AtHal3) that is related to plant growth and salt and, osmotic tolerance. AtHal3 shows sequence homology to ScHal3, a regulatory, subunit of the Saccharomyces cerevisae serine/threonine phosphatase PPz1., It has been proposed that AtHal3 and ScHal3 have similar roles in cellular, physiology, as Arabidopsis transgenic plants that overexpress AtHal3 and, yeast cells that overexpress ScHal3 display similar phenotypes of improved, salt tolerance. The enzymatic activity of AtHal3 has not been, investigated. However, the AtHal3 sequence is homologous to that of EpiD, a flavoprotein from Staphylococcus epidermidis that recognizes a peptidic, substrate and subsequently catalyzes the alpha, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10986463 (full description)]]
<StructureSection load='1e20' size='340' side='right'caption='[[1e20]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1e20]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E20 FirstGlance]. <br>
1E20 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]] with NI, FMN and BME as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E20 OCA]].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.02&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e20 OCA], [https://pdbe.org/1e20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e20 RCSB], [https://www.ebi.ac.uk/pdbsum/1e20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e20 ProSAT]</span></td></tr>
The X-ray structure of the FMN-binding protein AtHal3 provides the structural basis for the activity of a regulatory subunit involved in signal transduction., Albert A, Martinez-Ripoll M, Espinosa-Ruiz A, Yenush L, Culianez-Macia FA, Serrano R, Structure. 2000 Sep 15;8(9):961-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10986463 10986463]
</table>
== Function ==
[https://www.uniprot.org/uniprot/HAL3A_ARATH HAL3A_ARATH] Involved in plant growth and salt and osmotic tolerance. Catalyzes the decarboxylation of 4'-phosphopantothenoylcysteine to 4'-phosphopantetheine, a key step in coenzyme A biosynthesis. The enzyme is also able to decarboxylate pantothenoylcysteine to pantothenoylcysteamine.<ref>PMID:12860978</ref> <ref>PMID:16415216</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/e2/1e20_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=1e20 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Albert, A.]]
[[Category: Albert A]]
[[Category: Culianez-Macia, F.A.]]
[[Category: Culianez-Macia FA]]
[[Category: Espinosa-Ruiz, A.]]
[[Category: Espinosa-Ruiz A]]
[[Category: Martinez-Ripoll, M.]]
[[Category: Martinez-Ripoll M]]
[[Category: Serrano, R.]]
[[Category: Serrano R]]
[[Category: Yenush, L.]]
[[Category: Yenush L]]
[[Category: BME]]
[[Category: FMN]]
[[Category: NI]]
[[Category: flavoprotein]]
[[Category: regulation]]
[[Category: signal transduction]]
[[Category: stress]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:29:07 2007''

Latest revision as of 12:57, 20 March 2024

The FMN binding protein AtHal3The FMN binding protein AtHal3

Structural highlights

1e20 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.02Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HAL3A_ARATH Involved in plant growth and salt and osmotic tolerance. Catalyzes the decarboxylation of 4'-phosphopantothenoylcysteine to 4'-phosphopantetheine, a key step in coenzyme A biosynthesis. The enzyme is also able to decarboxylate pantothenoylcysteine to pantothenoylcysteamine.[1] [2]

Evolutionary Conservation

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

References

  1. ↑ Kupke T, Hernandez-Acosta P, Culianez-Macia FA. 4'-phosphopantetheine and coenzyme A biosynthesis in plants. J Biol Chem. 2003 Oct 3;278(40):38229-37. Epub 2003 Jul 14. PMID:12860978 doi:http://dx.doi.org/10.1074/jbc.M306321200
  2. ↑ Rubio S, Larson TR, Gonzalez-Guzman M, Alejandro S, Graham IA, Serrano R, Rodriguez PL. An Arabidopsis mutant impaired in coenzyme A biosynthesis is sugar dependent for seedling establishment. Plant Physiol. 2006 Mar;140(3):830-43. Epub 2006 Jan 13. PMID:16415216 doi:http://dx.doi.org/10.1104/pp.105.072066

1e20, resolution 2.02Å

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