8IOE
Cryo-EM structure of cyanobacteria phosphoketolase in dodecameric assembly
8IOE の概要
エントリーDOI | 10.2210/pdb8ioe/pdb |
EMDBエントリー | 35617 |
分子名称 | Probable phosphoketolase, THIAMINE DIPHOSPHATE, MAGNESIUM ION (3 entities in total) |
機能のキーワード | carbon metabolism, tpp-dependent enzyme, cytosolic protein |
由来する生物種 | Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) |
タンパク質・核酸の鎖数 | 12 |
化学式量合計 | 1074993.96 |
構造登録者 | |
主引用文献 | Lu, K.J.,Chang, C.W.,Wang, C.H.,Chen, F.Y.,Huang, I.Y.,Huang, P.H.,Yang, C.H.,Wu, H.Y.,Wu, W.J.,Hsu, K.C.,Ho, M.C.,Tsai, M.D.,Liao, J.C. An ATP-sensitive phosphoketolase regulates carbon fixation in cyanobacteria. Nat Metab, 5:1111-1126, 2023 Cited by PubMed Abstract: Regulation of CO fixation in cyanobacteria is important both for the organism and global carbon balance. Here we show that phosphoketolase in Synechococcus elongatus PCC7942 (SeXPK) possesses a distinct ATP-sensing mechanism, where a drop in ATP level allows SeXPK to divert precursors of the RuBisCO substrate away from the Calvin-Benson-Bassham cycle. Deleting the SeXPK gene increased CO fixation particularly during light-dark transitions. In high-density cultures, the Δxpk strain showed a 60% increase in carbon fixation and unexpectedly resulted in sucrose secretion without any pathway engineering. Using cryo-EM analysis, we discovered that these functions were enabled by a unique allosteric regulatory site involving two subunits jointly binding two ATP, which constantly suppresses the activity of SeXPK until the ATP level drops. This magnesium-independent ATP allosteric site is present in many species across all three domains of life, where it may also play important regulatory functions. PubMed: 37349485DOI: 10.1038/s42255-023-00831-w 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.86 Å) |
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