8f9y

From Proteopedia

(Difference between revisions)

Revision as of 07:09, 18 January 2023

SAL1 from Arabidopsis thaliana

Structural highlights

8f9y is a 1 chain structure with sequence from Arabidopsis thaliana. This structure supersedes the now removed PDB entry 5esy. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DPNP1_ARATH Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. May play a role in the biosynthesis of sulfate conjugates and RNA processing. Is also able to hydrolyze inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate. Could be considered as a negative regulator of abscisic acid (ABA)- and stress-responsive genes, through modulating the inositol 1,4,5-trisphosphate (IP3) turnover. Is also involved in salt tolerance. Acts as a suppressor of virus- and transgene-induced silencing.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Intracellular signaling during oxidative stress is complex, with organelle-to-nucleus retrograde communication pathways ill-defined or incomplete. Here we identify the 3'-phosphoadenosine 5'-phosphate (PAP) phosphatase SAL1 as a previously unidentified and conserved oxidative stress sensor in plant chloroplasts. Arabidopsis thaliana SAL1 (AtSAL1) senses changes in photosynthetic redox poise, hydrogen peroxide, and superoxide concentrations in chloroplasts via redox regulatory mechanisms. AtSAL1 phosphatase activity is suppressed by dimerization, intramolecular disulfide formation, and glutathionylation, allowing accumulation of its substrate, PAP, a chloroplast stress retrograde signal that regulates expression of plastid redox associated nuclear genes (PRANGs). This redox regulation of SAL1 for activation of chloroplast signaling is conserved in the plant kingdom, and the plant protein has evolved enhanced redox sensitivity compared with its yeast ortholog. Our results indicate that in addition to sulfur metabolism, SAL1 orthologs have evolved secondary functions in oxidative stress sensing in the plant kingdom.

Sensing and signaling of oxidative stress in chloroplasts by inactivation of the SAL1 phosphoadenosine phosphatase.,Chan KX, Mabbitt PD, Phua SY, Mueller JW, Nisar N, Gigolashvili T, Stroeher E, Grassl J, Arlt W, Estavillo GM, Jackson CJ, Pogson BJ Proc Natl Acad Sci U S A. 2016 Aug 2;113(31):E4567-E4576. Epub 2016 Jul 18. PMID:27432987^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Xiong L, Lee Bh, Ishitani M, Lee H, Zhang C, Zhu JK. FIERY1 encoding an inositol polyphosphate 1-phosphatase is a negative regulator of abscisic acid and stress signaling in Arabidopsis. Genes Dev. 2001 Aug 1;15(15):1971-84. PMID:11485991 doi:http://dx.doi.org/10.1101/gad.891901
↑ Gy I, Gasciolli V, Lauressergues D, Morel JB, Gombert J, Proux F, Proux C, Vaucheret H, Mallory AC. Arabidopsis FIERY1, XRN2, and XRN3 are endogenous RNA silencing suppressors. Plant Cell. 2007 Nov;19(11):3451-61. Epub 2007 Nov 9. PMID:17993620 doi:http://dx.doi.org/10.1105/tpc.107.055319
↑ Quintero FJ, Garciadeblas B, Rodriguez-Navarro A. The SAL1 gene of Arabidopsis, encoding an enzyme with 3'(2'),5'-bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase activities, increases salt tolerance in yeast. Plant Cell. 1996 Mar;8(3):529-37. PMID:8721754
↑ Chan KX, Mabbitt PD, Phua SY, Mueller JW, Nisar N, Gigolashvili T, Stroeher E, Grassl J, Arlt W, Estavillo GM, Jackson CJ, Pogson BJ. Sensing and signaling of oxidative stress in chloroplasts by inactivation of the SAL1 phosphoadenosine phosphatase. Proc Natl Acad Sci U S A. 2016 Aug 2;113(31):E4567-E4576. Epub 2016 Jul 18. PMID:27432987 doi:http://dx.doi.org/10.1073/pnas.1604936113

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8f9y"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8f9y is ON HOLD
+==SAL1 from Arabidopsis thaliana==
+<StructureSection load='8f9y' size='340' side='right'caption='[[8f9y]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8f9y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5esy 5esy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F9Y FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=8f9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f9y OCA], [https://pdbe.org/8f9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f9y RCSB], [https://www.ebi.ac.uk/pdbsum/8f9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f9y ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DPNP1_ARATH DPNP1_ARATH] Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. May play a role in the biosynthesis of sulfate conjugates and RNA processing. Is also able to hydrolyze inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate. Could be considered as a negative regulator of abscisic acid (ABA)- and stress-responsive genes, through modulating the inositol 1,4,5-trisphosphate (IP3) turnover. Is also involved in salt tolerance. Acts as a suppressor of virus- and transgene-induced silencing.<ref>PMID:11485991</ref> <ref>PMID:17993620</ref> <ref>PMID:8721754</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Intracellular signaling during oxidative stress is complex, with organelle-to-nucleus retrograde communication pathways ill-defined or incomplete. Here we identify the 3'-phosphoadenosine 5'-phosphate (PAP) phosphatase SAL1 as a previously unidentified and conserved oxidative stress sensor in plant chloroplasts. Arabidopsis thaliana SAL1 (AtSAL1) senses changes in photosynthetic redox poise, hydrogen peroxide, and superoxide concentrations in chloroplasts via redox regulatory mechanisms. AtSAL1 phosphatase activity is suppressed by dimerization, intramolecular disulfide formation, and glutathionylation, allowing accumulation of its substrate, PAP, a chloroplast stress retrograde signal that regulates expression of plastid redox associated nuclear genes (PRANGs). This redox regulation of SAL1 for activation of chloroplast signaling is conserved in the plant kingdom, and the plant protein has evolved enhanced redox sensitivity compared with its yeast ortholog. Our results indicate that in addition to sulfur metabolism, SAL1 orthologs have evolved secondary functions in oxidative stress sensing in the plant kingdom.
-Authors: Frkic, R.L., Kaczmarski, J.A., Tan, L., Jackson, C.J.
+Sensing and signaling of oxidative stress in chloroplasts by inactivation of the SAL1 phosphoadenosine phosphatase.,Chan KX, Mabbitt PD, Phua SY, Mueller JW, Nisar N, Gigolashvili T, Stroeher E, Grassl J, Arlt W, Estavillo GM, Jackson CJ, Pogson BJ Proc Natl Acad Sci U S A. 2016 Aug 2;113(31):E4567-E4576. Epub 2016 Jul 18. PMID:27432987<ref>PMID:27432987</ref>
-Description: SAL1 from Arabidopsis thaliana
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Kaczmarski, J.A]]
+<div class="pdbe-citations 8f9y" style="background-color:#fffaf0;"></div>
-[[Category: Jackson, C.J]]
+== References ==
-[[Category: Tan, L]]
+<references/>
-[[Category: Frkic, R.L]]
+__TOC__
+</StructureSection>
+[[Category: Arabidopsis thaliana]]
+[[Category: Large Structures]]
+[[Category: Frkic RL]]
+[[Category: Jackson CJ]]
+[[Category: Kaczmarski JA]]
+[[Category: Tan L]]

8f9y

From Proteopedia

Revision as of 07:09, 18 January 2023

SAL1 from Arabidopsis thaliana

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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