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- EMDB-9882: Co-purified Fatty Acid Synthase -

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Basic information

Entry
Database: EMDB / ID: EMD-9882
TitleCo-purified Fatty Acid Synthase
Map data
Sample
  • Complex: Co-purified Fatty acid sythase
    • Protein or peptide: Fatty acid synthase subunit beta
    • Protein or peptide: Fatty acid synthase subunit alpha
    • Protein or peptide: Fatty acid synthase subunit alpha
Keywordsco-purified / ACP domains / AT domains / TRANSFERASE
Function / homology
Function and homology information


: / fatty-acyl-CoA synthase system / : / fatty-acyl-CoA synthase activity / fatty acid synthase complex / (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity / [acyl-carrier-protein] S-acetyltransferase / palmitoyltransferase activity / [acyl-carrier-protein] S-acetyltransferase activity / oleoyl-[acyl-carrier-protein] hydrolase ...: / fatty-acyl-CoA synthase system / : / fatty-acyl-CoA synthase activity / fatty acid synthase complex / (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity / [acyl-carrier-protein] S-acetyltransferase / palmitoyltransferase activity / [acyl-carrier-protein] S-acetyltransferase activity / oleoyl-[acyl-carrier-protein] hydrolase / (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity / holo-[acyl-carrier-protein] synthase activity / [acyl-carrier-protein] S-malonyltransferase / [acyl-carrier-protein] S-malonyltransferase activity / fatty acid synthase activity / 3-hydroxyacyl-[acyl-carrier-protein] dehydratase / (3R)-3-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity / beta-ketoacyl-[acyl-carrier-protein] synthase I / 3-oxoacyl-[acyl-carrier-protein] reductase / 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity / enoyl-[acyl-carrier-protein] reductase (NADH) / long-chain fatty acid biosynthetic process / enoyl-[acyl-carrier-protein] reductase (NADH) activity / 3-oxoacyl-[acyl-carrier-protein] synthase activity / lipid droplet / magnesium ion binding / mitochondrion / cytosol / cytoplasm
Similarity search - Function
: / Fatty acid synthase, meander beta sheet domain / Fatty acid synthase subunit beta, N-terminal domain / N-terminal domain in fatty acid synthase subunit beta / Fatty acid synthase meander beta sheet domain / Fatty acid synthase beta subunit AflB /Fas1-like, fungi / Fatty acid synthase subunit alpha, acyl carrier domain / Fatty acid synthase subunit alpha Acyl carrier domain / Fatty acid synthase beta subunit AflB /Fas1-like, central domain / Fatty acid synthase alpha subunit, yeast ...: / Fatty acid synthase, meander beta sheet domain / Fatty acid synthase subunit beta, N-terminal domain / N-terminal domain in fatty acid synthase subunit beta / Fatty acid synthase meander beta sheet domain / Fatty acid synthase beta subunit AflB /Fas1-like, fungi / Fatty acid synthase subunit alpha, acyl carrier domain / Fatty acid synthase subunit alpha Acyl carrier domain / Fatty acid synthase beta subunit AflB /Fas1-like, central domain / Fatty acid synthase alpha subunit, yeast / Fatty acid synthase subunit beta/Fas1-like, helical / Fatty acid synthase type I, helical / Fatty acid synthase type I helical domain / Fatty acid synthase / N-terminal of MaoC-like dehydratase / N-terminal half of MaoC dehydratase / Starter unit:ACP transacylase / Starter unit:ACP transacylase in aflatoxin biosynthesis / Holo-[acyl carrier protein] synthase / Phosphopantetheine-protein transferase domain / MaoC-like dehydratase domain / MaoC like domain / 4'-phosphopantetheinyl transferase domain / 4'-phosphopantetheinyl transferase domain superfamily / 4'-phosphopantetheinyl transferase superfamily / HotDog domain superfamily / Acyl transferase domain superfamily / Acyl transferase / Acyl transferase domain / Acyl transferase domain in polyketide synthase (PKS) enzymes. / Acyl transferase/acyl hydrolase/lysophospholipase / Ketosynthase family 3 (KS3) domain profile. / Beta-ketoacyl synthase, active site / Ketosynthase family 3 (KS3) active site signature. / Polyketide synthase, beta-ketoacyl synthase domain / Beta-ketoacyl synthase, N-terminal / Beta-ketoacyl synthase, C-terminal / Beta-ketoacyl synthase, N-terminal domain / Beta-ketoacyl synthase, C-terminal domain / Phosphopantetheine attachment site. / Thiolase-like / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / Aldolase-type TIM barrel / NAD(P)-binding domain superfamily
Similarity search - Domain/homology
Fatty acid synthase subunit beta / Fatty acid synthase subunit alpha
Similarity search - Component
Biological speciesSchizosaccharomyces pombe (fission yeast) / Saccharomyces cerevisiae (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.7 Å
AuthorsQiu SW / Liu S
Funding support China, 1 items
OrganizationGrant numberCountry
National Basic Research Program of China (973 Program) China
CitationJournal: J Mol Cell Biol / Year: 2019
Title: Modulation of fatty acid synthase by ATR checkpoint kinase Rad3.
Authors: Shuwan Qiu / Sheng Liu / Zannati Ferdous Zaoti / Xuejuan Wang / Gang Cai /
History
DepositionApr 8, 2019-
Header (metadata) releaseSep 25, 2019-
Map releaseSep 25, 2019-
UpdateApr 24, 2024-
Current statusApr 24, 2024Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0215
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.0215
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6jsi
  • Surface level: 0.0215
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6jsi
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_9882.png

Downloads & links

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Map

FileDownload / File: emd_9882.map.gz / Format: CCP4 / Size: 144.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.35 Å
Density
Contour LevelBy AUTHOR: 0.0215 / Movie #1: 0.0215
Minimum - Maximum-0.08262251 - 0.16006076
Average (Standard dev.)0.0010062658 (±0.0070240693)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions336336336
Spacing336336336
CellA=B=C: 453.6 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.351.351.35
M x/y/z336336336
origin x/y/z0.0000.0000.000
length x/y/z453.600453.600453.600
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ858858858
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS336336336
D min/max/mean-0.0830.1600.001

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Supplemental data

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Sample components

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Entire : Co-purified Fatty acid sythase

EntireName: Co-purified Fatty acid sythase
Components
  • Complex: Co-purified Fatty acid sythase
    • Protein or peptide: Fatty acid synthase subunit beta
    • Protein or peptide: Fatty acid synthase subunit alpha
    • Protein or peptide: Fatty acid synthase subunit alpha

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Supramolecule #1: Co-purified Fatty acid sythase

SupramoleculeName: Co-purified Fatty acid sythase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Schizosaccharomyces pombe (fission yeast)

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Macromolecule #1: Fatty acid synthase subunit beta

MacromoleculeName: Fatty acid synthase subunit beta / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 200.852922 KDa
SequenceString: MDAYSTRPLT LSHGSLEHVL LVPTASFFIA SQLQEQFNKI LPEPTEGFAA DDEPTTPAEL VGKFLGYVSS LVEPSKVGQF DQVLNLCLT EFENCYLEGN DIHALAAKLL QENDTTLVKT KELIKNYITA RIMAKRPFDK KSNSALFRAV GEGNAQLVAI F GGQGNTDD ...String:
MDAYSTRPLT LSHGSLEHVL LVPTASFFIA SQLQEQFNKI LPEPTEGFAA DDEPTTPAEL VGKFLGYVSS LVEPSKVGQF DQVLNLCLT EFENCYLEGN DIHALAAKLL QENDTTLVKT KELIKNYITA RIMAKRPFDK KSNSALFRAV GEGNAQLVAI F GGQGNTDD YFEELRDLYQ TYHVLVGDLI KFSAETLSEL IRTTLDAEKV FTQGLNILEW LENPSNTPDK DYLLSIPISC PL IGVIQLA HYVVTAKLLG FTPGELRSYL KGATGHSQGL VTAVAIAETD SWESFFVSVR KAITVLFFIG VRCYEAYPNT SLP PSILED SLENNEGVPS PMLSISNLTQ EQVQDYVNKT NSHLPAGKQV EISLVNGAKN LVVSGPPQSL YGLNLTLRKA KAPS GLDQS RIPFSERKLK FSNRFLPVAS PFHSHLLVPA SDLINKDLVK NNVSFNAKDI QIPVYDTFDG SDLRVLSGSI SERIV DCII RLPVKWETTT QFKATHILDF GPGGASGLGV LTHRNKDGTG VRVIVAGTLD INPDDDYGFK QEIFDVTSNG LKKNPN WLE EYHPKLIKNK S(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) 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(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)VLP NTALKTSIQH VGMINGRKLI KFETRNEDDV VVLTGEAEIE QPVTTFVFTG QGSQEQG MG MDLYKTSKAA QDVWNRADNH FKDTYGFSIL DIVINNPVNL TIHFGGEKGK RIRENYSAMI FETIVDGKLK TEKIFKEI N EHSTSYTFRS EKGLLSATQF TQPALTLMEK AAFEDLKSKG LIPADATFAG HSLGEYAALA SLADVMSIES LVEVVFYRG MTMQVAVPRD ELGRSNYGMI AINPGRVAAS FSQEALQYVV ERVGKRTGWL VEIVNYNVEN QQYVAAGDLR ALDTVTNVLN FIKLQKIDI IELQKSLSLE EVEGHLFEII DEASKKSAVK PRPLKLERGF ACIPLVGISV PFHSTYLMNG VKPFKSFLKK N IIKENVKV ARLAGKYIPN LTAKPFQVTK EYFQDVYDLT GSEPIKEIID NWEKYEQS

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Macromolecule #2: Fatty acid synthase subunit alpha

MacromoleculeName: Fatty acid synthase subunit alpha / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 186.482422 KDa
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) 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LTNILRMMG CVKKQKSARG IETRPAQVIL PMSPNHGTFG GDGMYSESKL SLETLFNRWH SESWANQLTV CGAIIGWTRG TGLMSANNII AEGIEKMGV RTFSQKEMAF NLLGLLTPEV VELCQKSPVM ADLNGGLQFV PELKEFTAKL RKELVETSEV RKAVSIETAL E HKVVNGNS ADAAYAQVEI QPRANIQLDF PELKPYKQVK QIAPAELEGL LDLERVIVVT GFAEVGPWGS ARTRWEMEAF GE FSLEGCV EMAWIMGFIS YHNGNLKGRP YTGWVDSKTK EPVDDKDVKA KYETSILEHS GIRLIEPELF NGYNPEKKEM IQE VIVEED LEPFEASKET AEQFKHQHGD KVDIFEIPET GEYSVKLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI SDDI ISQVD PITLFVLVSV VEAFIASGIT DPYEMYKYVH VSEVGNCSGS GMGGVSALRG MFKDRFKDEP VQNDILQESF INTMS AWVN MLLISSSGPI KTPVGACATS VESVDIGVET ILSGKARICI VGGYDDFQEE GSFEFGNMKA TSNTLEEFEH GRTPAE MSR PATTTRNGFM EAQGAGIQII MQADLALKMG VPIYGIVAMA ATATDKIGRS VPAPGKGILT TAREHHSSVK YASPNLN MK YRKRQLVTRE AQIKDWVENE LEALKLEAEE IPSEDQNEFL LERTREIHNE AESQLRAAQQ QWGNDFYKRD PRI(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) 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Macromolecule #3: Fatty acid synthase subunit alpha

MacromoleculeName: Fatty acid synthase subunit alpha / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 8.631504 KDa
SequenceString:
LNMKYRKRQL VTREAQIKDW VENELEALKL EAEEIPSEDQ NEFLLERTRE IHNEAESQLR AAQQQWGNDF Y

UniProtKB: Fatty acid synthase subunit alpha

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 1.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: EMDB MAP
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
Final reconstructionApplied symmetry - Point group: D3 (2x3 fold dihedral) / Resolution.type: BY AUTHOR / Resolution: 4.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 3692

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