5A5L

Structure of dual function FBPase SBPase from Thermosynechococcus elongatus

Summary for 5A5L

• Entry DOI: 10.2210/pdb5a5l/pdb
• Descriptor: D-FRUCTOSE 1,6-BISPHOSPHATASE CLASS 2/SEDOHEPTULOSE 1,7-BISPHOSPHATASE, PHOSPHATE ION, 7-O-phosphono-alpha-L-galacto-hept-2-ulopyranose, ... (5 entities in total)
• Functional Keywords: hydrolase, calvin cycle, cyanobacteria, phosphatase
• Biological source: THERMOSYNECHOCOCCUS ELONGATUS
• Total number of polymer chains: 1
• Total formula weight: 39920.24

Authors

Cotton, C.A.R.,Kabasakal, B.,Miah, N.,Murray, J.W. (deposition date: 2015-06-19, release date: 2015-10-14, Last modification date: 2024-11-06)

Primary citation

Cotton, C.A.R.,Kabasakal, B.,Miah, N.,Murray, J.W.
Structure of the Dual-Function Fructose-1,6/Sedoheptulose-1, 7-Bisphosphatase from Thermosynechococcus Elongatus Bound with Sedoheptulose-7-Phosphate.
Acta Crystallogr.,Sect.F, 71:1341-, 2015

PubMed Abstract: 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.

PubMed: 26457528
DOI: 10.1107/S2053230X15016829

Experimental method

X-RAY DIFFRACTION (2.34 Å)