5a5l

Structure of dual function FBPase SBPase from Thermosynechococcus elongatus

spinqualitylabelsall models 5a5l, resolution 2.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a5l is a 1 chain structure with sequence from Thermosynechococcus vestitus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, PO4, VTB Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FBSB_THEVB Catalyzes the hydrolysis of fructose 1,6-bisphosphate (Fru 1,6-P2) and sedoheptulose 1,7-bisphosphate (Sed 1,7-P2) to fructose 6-phosphate and sedoheptulose 7-phosphate, respectively. Publication Abstract from PubMed The dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase) in cyanobacteria carries out two activities in the Calvin cycle. Structures of this enzyme from the cyanobacterium Synechocystis sp. PCC 6803 exist, but only with adenosine monophosphate (AMP) or fructose-1,6-bisphosphate and AMP bound. The mechanisms which control both selectivity between the two sugars and the structural mechanisms for redox control are still unresolved. Here, the structure of the dual-function FBP/SBPase from the thermophilic cyanobacterium Thermosynechococcus elongatus is presented with sedoheptulose-7-phosphate bound and in the absence of AMP. The structure is globally very similar to the Synechocystis sp. PCC 6803 enzyme, but highlights features of selectivity at the active site and loop ordering at the AMP-binding site. Understanding the selectivity and control of this enzyme is critical for understanding the Calvin cycle in cyanobacteria and for possible biotechnological application in plants. Structure of the dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase from Thermosynechococcus elongatus bound with sedoheptulose-7-phosphate.,Cotton CA, Kabasakal BV, Miah NA, Murray JW Acta Crystallogr F Struct Biol Commun. 2015 Oct 1;71(Pt 10):1341-5. doi:, 10.1107/S2053230X15016829. Epub 2015 Sep 23. PMID:26457528 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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