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	Reconstruction of a fatty acid synthesis cycle from acyl carrier protein and cofactor structural snapshots.
Journal, issue, pages	Cell, Vol. 186, Issue 23, Page 5054-5067.e16, Year 2023
Publish date	Nov 9, 2023
Authors	Kashish Singh / Georg Bunzel / Benjamin Graf / Ka Man Yip / Meina Neumann-Schaal / Holger Stark / Ashwin Chari /
PubMed Abstract	Fatty acids (FAs) play a central metabolic role in living cells as constituents of membranes, cellular energy reserves, and second messenger precursors. A 2.6 MDa FA synthase (FAS), where the ...Fatty acids (FAs) play a central metabolic role in living cells as constituents of membranes, cellular energy reserves, and second messenger precursors. A 2.6 MDa FA synthase (FAS), where the enzymatic reactions and structures are known, is responsible for FA biosynthesis in yeast. Essential in the yeast FAS catalytic cycle is the acyl carrier protein (ACP) that actively shuttles substrates, biosynthetic intermediates, and products from one active site to another. We resolve the S. cerevisiae FAS structure at 1.9 Å, elucidating cofactors and water networks involved in their recognition. Structural snapshots of ACP domains bound to various enzymatic domains allow the reconstruction of a full yeast FA biosynthesis cycle. The structural information suggests that each FAS functional unit could accommodate exogenous proteins to incorporate various enzymatic activities, and we show proof-of-concept experiments where ectopic proteins are used to modulate FAS product profiles.
External links	Cell / PubMed:37949058
Methods	EM (single particle)
Resolution	1.9 - 4.0 Å
Structure data	17839 8prv EMDB-17839, PDB-8prv: Asymmetric unit of the yeast fatty acid synthase in the non-rotated state with ACP at the ketosreductase domain (FASamn sample) Method: EM (single particle) / Resolution: 2.9 Å 17840 8prw EMDB-17840, PDB-8prw: Cryo-EM structure of the yeast fatty acid synthase at 1.9 angstrom resolution Method: EM (single particle) / Resolution: 1.9 Å 17842 8ps1 EMDB-17842, PDB-8ps1: Asymmetric unit of the yeast fatty acid synthase in the non-rotated state with ACP at the ketosynthase domain (FASamn sample) Method: EM (single particle) / Resolution: 2.8 Å 17843 8ps2 EMDB-17843, PDB-8ps2: Asymmetric unit of the yeast fatty acid synthase with ACP at the enoyl reductase domain (FASam sample) Method: EM (single particle) / Resolution: 2.9 Å 17846 8ps8 EMDB-17846, PDB-8ps8: Asymmetric unit of the yeast fatty acid synthase in the semi non-rotated state with ACP at the enoyl reductase domain (FASam sample) Method: EM (single particle) / Resolution: 4.0 Å 17847 8ps9 EMDB-17847, PDB-8ps9: Asymmetric unit of the yeast fatty acid synthase in the non-rotated state with ACP at the ketosynthase domain (FASam sample) Method: EM (single particle) / Resolution: 2.9 Å 17848 8psa EMDB-17848, PDB-8psa: Asymmetric unit of the yeast fatty acid synthase in the semi non-rotated state with ACP at the ketosynthase domain (FASam sample) Method: EM (single particle) / Resolution: 3.6 Å 17851 8psf EMDB-17851, PDB-8psf: Asymmetric unit of the yeast fatty acid synthase in non-rotated state with ACP at the acetyl transferase domain (FASx sample) Method: EM (single particle) / Resolution: 2.8 Å 17852 8psg EMDB-17852, PDB-8psg: Asymmetric unit of the yeast fatty acid synthase in the semi non-rotated state with ACP at the acetyl transferase domain (FASx sample) Method: EM (single particle) / Resolution: 3.7 Å 17853 8psj EMDB-17853, PDB-8psj: Asymmetric unit of the yeast fatty acid synthase in the semi rotated state with ACP at the acetyl transferase domain (FASx sample) Method: EM (single particle) / Resolution: 3.4 Å 17854 8psk EMDB-17854, PDB-8psk: Asymmetric unit of the yeast fatty acid synthase in the non-rotated state with ACP at the ketosynthase domain (FASx sample) Method: EM (single particle) / Resolution: 2.8 Å 17855 8psl EMDB-17855, PDB-8psl: Asymmetric unit of the yeast fatty acid synthase in the semi non-rotated state with ACP at the ketosynthase domain (FASx sample) Method: EM (single particle) / Resolution: 3.7 Å 17856 8psm EMDB-17856, PDB-8psm: Asymmetric unit of the yeast fatty acid synthase in the non-rotated state with ACP at the malonyl/palmitoyl transferase domain (FASx sample) Method: EM (single particle) / Resolution: 3.1 Å 17859 8psp EMDB-17859, PDB-8psp: Asymmetric unit of the yeast fatty acid synthase in rotated state with ACP at the acetyl transferase domain (FASx sample) Method: EM (single particle) / Resolution: 2.9 Å
Chemicals	ChemComp-NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE ChemComp-A5S: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] 3-oxidanylidenebutanethioate ChemComp-FMN: FLAVIN MONONUCLEOTIDE ChemComp-COA: COENZYME A ChemComp-FNR: 1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL ChemComp-HOH: WATER ChemComp-A3Z: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (~{E})-but-2-enethioate ChemComp-MLC: MALONYL-COENZYME A ChemComp-PNS: 4'-PHOSPHOPANTETHEINE
Source	saccharomyces cerevisiae (brewer's yeast)
Keywords	CYTOSOLIC PROTEIN / Fatty acid synthase / acyl carrier protein / FAS / ACP