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| | <StructureSection load='6rng' size='340' side='right'caption='[[6rng]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='6rng' size='340' side='right'caption='[[6rng]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6rng]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RNG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RNG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rng]] 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=6RNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RNG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <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]] 2.15Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FBA6, At2g36460 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <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=6rng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rng OCA], [https://pdbe.org/6rng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rng RCSB], [https://www.ebi.ac.uk/pdbsum/6rng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rng ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6rng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rng OCA], [http://pdbe.org/6rng PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rng RCSB], [http://www.ebi.ac.uk/pdbsum/6rng PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rng 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== | | ==See Also== |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Fructose-bisphosphate aldolase]]
| + | |
| | [[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]]
| + | |
| Structural highlights
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
- ↑ 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
- ↑ 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
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