5el8: Difference between revisions

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'''Unreleased structure'''


The entry 5el8 is ON HOLD  until Paper Publication
==The structure of DHAR1 from Arabidopsis thaliana==
<StructureSection load='5el8' size='340' side='right'caption='[[5el8]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5el8]] 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=5EL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EL8 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5el8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5el8 OCA], [https://pdbe.org/5el8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5el8 RCSB], [https://www.ebi.ac.uk/pdbsum/5el8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5el8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DHAR1_ARATH DHAR1_ARATH] Displays a dual function. As a soluble protein, exhibits glutathione-dependent thiol transferase and dehydroascorbate (DHA) reductase activities. Key component of the ascorbate recycling system. Involved in the redox homeostasis, especially in scavenging of ROS under oxidative stresses, subsequently to biotic or abiotic inducers. As a peripheral membrane protein, could also function as voltage-gated ion channel.<ref>PMID:12077129</ref> <ref>PMID:16262714</ref> <ref>PMID:17267397</ref>


Authors:  
==See Also==
 
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
Description:  
== References ==
[[Category: Unreleased Structures]]
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Lapthorn AJ]]
[[Category: Menault M]]
[[Category: Roszak AW]]

Latest revision as of 09:32, 5 July 2023

The structure of DHAR1 from Arabidopsis thalianaThe structure of DHAR1 from Arabidopsis thaliana

Structural highlights

5el8 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 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DHAR1_ARATH Displays a dual function. As a soluble protein, exhibits glutathione-dependent thiol transferase and dehydroascorbate (DHA) reductase activities. Key component of the ascorbate recycling system. Involved in the redox homeostasis, especially in scavenging of ROS under oxidative stresses, subsequently to biotic or abiotic inducers. As a peripheral membrane protein, could also function as voltage-gated ion channel.[1] [2] [3]

See Also

References

  1. ↑ Dixon DP, Davis BG, Edwards R. Functional divergence in the glutathione transferase superfamily in plants. Identification of two classes with putative functions in redox homeostasis in Arabidopsis thaliana. J Biol Chem. 2002 Aug 23;277(34):30859-69. Epub 2002 Jun 19. PMID:12077129 doi:http://dx.doi.org/10.1074/jbc.M202919200
  2. ↑ Sasaki-Sekimoto Y, Taki N, Obayashi T, Aono M, Matsumoto F, Sakurai N, Suzuki H, Hirai MY, Noji M, Saito K, Masuda T, Takamiya K, Shibata D, Ohta H. Coordinated activation of metabolic pathways for antioxidants and defence compounds by jasmonates and their roles in stress tolerance in Arabidopsis. Plant J. 2005 Nov;44(4):653-68. PMID:16262714 doi:http://dx.doi.org/10.1111/j.1365-313X.2005.02560.x
  3. ↑ Elter A, Hartel A, Sieben C, Hertel B, Fischer-Schliebs E, Luttge U, Moroni A, Thiel G. A plant homolog of animal chloride intracellular channels (CLICs) generates an ion conductance in heterologous systems. J Biol Chem. 2007 Mar 23;282(12):8786-92. Epub 2007 Jan 31. PMID:17267397 doi:http://dx.doi.org/10.1074/jbc.M607241200

5el8, resolution 2.30Å

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