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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