Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	An ATP-sensitive phosphoketolase regulates carbon fixation in cyanobacteria.
Journal, issue, pages	Nat Metab, Vol. 5, Issue 7, Page 1111-1126, Year 2023
Publish date	Jun 22, 2023
Authors	Kuan-Jen Lu / Chiung-Wen Chang / Chun-Hsiung Wang / Frederic Y-H Chen / Irene Y Huang / Pin-Hsuan Huang / Cheng-Han Yang / Hsiang-Yi Wu / Wen-Jin Wu / Kai-Cheng Hsu / Meng-Chiao Ho / Ming-Daw Tsai / James C Liao /
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 ...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.
External links	Nat Metab / PubMed:37349485 / PubMed Central
Methods	EM (single particle)
Resolution	2.17 - 2.86 Å
Structure data	35609 8io6 EMDB-35609, PDB-8io6: Cryo-EM structure of phosphoketolase from Bifidobacterium longum in octameric assembly Method: EM (single particle) / Resolution: 2.68 Å 35610 8io7 EMDB-35610, PDB-8io7: Cryo-EM structure of phosphoketolase from Bifidobacterium longum in dimeric assembly Method: EM (single particle) / Resolution: 2.62 Å 35611 8io8 EMDB-35611: Cryo-EM structure of cyanobacteria phosphoketolase complexed with AMPPNP in dimeric assembly PDB-8io8: Cryo-EM structure of cyanobacteria phosphoketolase complexed with AMPPNPin dimeric assembly Method: EM (single particle) / Resolution: 2.17 Å 35612 8io9 EMDB-35612: Cryo-EM structure of cyanobacteria phosphoketolase complexed with AMPPNPin dodecameric assembly PDB-8io9: Cryo-EM structure of cyanobacteria phosphoketolase complexed with AMPPNP in dodecameric assembly Method: EM (single particle) / Resolution: 2.36 Å 35613 8ioa EMDB-35613, PDB-8ioa: Cryo-EM structure of cyanobacteria phosphoketolase Method: EM (single particle) / Resolution: 2.63 Å 35617 8ioe EMDB-35617, PDB-8ioe: Cryo-EM structure of cyanobacteria phosphoketolase in dodecameric assembly Method: EM (single particle) / Resolution: 2.86 Å
Chemicals	ChemComp-TPP: THIAMINE DIPHOSPHATE ChemComp-MG: Unknown entry ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM
Source	Bifidobacteriaceae bacterium (bacteria) bifidobacterium longum subsp. longum f8 (bacteria) Synechococcus (bacteria) synechococcus elongatus (strain atcc 33912 / pcc 7942 / fachb-805) (bacteria)
Keywords	CYTOSOLIC PROTEIN / Carbon metabolism / TPP-dependent enzyme