5A5L

Structure of dual function FBPase SBPase from Thermosynechococcus elongatus

5A5L の概要

• エントリーDOI: 10.2210/pdb5a5l/pdb
• 分子名称: 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)
• 機能のキーワード: hydrolase, calvin cycle, cyanobacteria, phosphatase
• 由来する生物種: THERMOSYNECHOCOCCUS ELONGATUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39920.24

構造登録者

Cotton, C.A.R.,Kabasakal, B.,Miah, N.,Murray, J.W. (登録日: 2015-06-19, 公開日: 2015-10-14, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.34 Å)