5a5l
From Proteopedia
Structure of dual function FBPase SBPase from Thermosynechococcus elongatus
Structural highlights
FunctionFBSB_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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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