6rs1: Difference between revisions

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<StructureSection load='6rs1' size='340' side='right'caption='[[6rs1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='6rs1' size='340' side='right'caption='[[6rs1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6rs1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RS1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RS1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6rs1]] is a 4 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=6RS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RS1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6rng|6rng]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] </span></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=6rs1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rs1 OCA], [https://pdbe.org/6rs1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rs1 RCSB], [https://www.ebi.ac.uk/pdbsum/6rs1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rs1 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6rs1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rs1 OCA], [http://pdbe.org/6rs1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rs1 RCSB], [http://www.ebi.ac.uk/pdbsum/6rs1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rs1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ALFC6_ARATH ALFC6_ARATH]] Fructose-bisphosphate aldolase that plays a key role in glycolysis and gluconeogenesis (PubMed:21782461). Associates with GAPC1 to the outer mitochondrial membrane, in a redox-dependent manner, leading to binding and bundling of actin. Actin binding and bundling occurs under oxidizing conditions and is reversible under reducing conditions. May be part of a redox-dependent retrograde signal transduction network for adaptation upon oxidative stress (PubMed:23316205).<ref>PMID:21782461</ref> <ref>PMID:23316205</ref>
[https://www.uniprot.org/uniprot/ALFC6_ARATH ALFC6_ARATH] Fructose-bisphosphate aldolase that plays a key role in glycolysis and gluconeogenesis (PubMed:21782461). Associates with GAPC1 to the outer mitochondrial membrane, in a redox-dependent manner, leading to binding and bundling of actin. Actin binding and bundling occurs under oxidizing conditions and is reversible under reducing conditions. May be part of a redox-dependent retrograde signal transduction network for adaptation upon oxidative stress (PubMed:23316205).<ref>PMID:21782461</ref> <ref>PMID:23316205</ref>  
 
==See Also==
*[[Aldolase 3D structures|Aldolase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Fructose-bisphosphate aldolase]]
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Shahar, A]]
[[Category: Shahar A]]
[[Category: Skirycz, A]]
[[Category: Skirycz A]]
[[Category: Wojciechowska, I]]
[[Category: Wojciechowska I]]
[[Category: Zarivach, R]]
[[Category: Zarivach R]]
[[Category: Peptide binding protein]]

Latest revision as of 15:27, 24 January 2024

Dipeptide Gly-Pro binds to a glycolytic enzyme fructose bisphosphate aldolaseDipeptide Gly-Pro binds to a glycolytic enzyme fructose bisphosphate aldolase

Structural highlights

6rs1 is a 4 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 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALFC6_ARATH Fructose-bisphosphate aldolase that plays a key role in glycolysis and gluconeogenesis (PubMed:21782461). Associates with GAPC1 to the outer mitochondrial membrane, in a redox-dependent manner, leading to binding and bundling of actin. Actin binding and bundling occurs under oxidizing conditions and is reversible under reducing conditions. May be part of a redox-dependent retrograde signal transduction network for adaptation upon oxidative stress (PubMed:23316205).[1] [2]

See Also

References

  1. ↑ van der Linde K, Gutsche N, Leffers HM, Lindermayr C, Muller B, Holtgrefe S, Scheibe R. Regulation of plant cytosolic aldolase functions by redox-modifications. Plant Physiol Biochem. 2011 Sep;49(9):946-57. doi: 10.1016/j.plaphy.2011.06.009. , Epub 2011 Jul 3. PMID:21782461 doi:http://dx.doi.org/10.1016/j.plaphy.2011.06.009
  2. ↑ Wojtera-Kwiczor J, Gross F, Leffers HM, Kang M, Schneider M, Scheibe R. Transfer of a Redox-Signal through the Cytosol by Redox-Dependent Microcompartmentation of Glycolytic Enzymes at Mitochondria and Actin Cytoskeleton. Front Plant Sci. 2013 Jan 9;3:284. doi: 10.3389/fpls.2012.00284. eCollection, 2012. PMID:23316205 doi:http://dx.doi.org/10.3389/fpls.2012.00284

6rs1, resolution 1.90Å

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