2CDH

ARCHITECTURE OF THE THERMOMYCES LANUGINOSUS FUNGAL FATTY ACID SYNTHASE AT 5 ANGSTROM RESOLUTION.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.20 Å

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Architecture of a Fungal Fatty Acid Synthase at 5 A Resolution.

Jenni, S.Leibundgut, M.Maier, T.Ban, N.

(2006) Science 311: 1263

  • DOI: https://doi.org/10.1126/science.1123251
  • Primary Citation of Related Structures:  
    2CDH

  • PubMed Abstract: 

    All steps of fatty acid synthesis in fungi are catalyzed by the fatty acid synthase, which forms a 2.6-megadalton alpha6beta6 complex. We have determined the molecular architecture of this multienzyme by fitting the structures of homologous enzymes that catalyze the individual steps of the reaction pathway into a 5 angstrom x-ray crystallographic electron density map. The huge assembly contains two separated reaction chambers, each equipped with three sets of active sites separated by distances up to approximately 130 angstroms, across which acyl carrier protein shuttles substrates during the reaction cycle. Regions of the electron density arising from well-defined structural features outside the catalytic domains separate the two reaction chambers and serve as a matrix in which domains carrying the various active sites are embedded. The structure rationalizes the compartmentalization of fatty acid synthesis, and the spatial arrangement of the active sites has specific implications for our understanding of the reaction cycle mechanism and of the architecture of multienzymes in general.


  • Organizational Affiliation

    Institute of Molecular Biology and Biophysics, Department of Biology, Swiss Federal Institute of Technology (ETH Zurich), 8093 Zurich, Switzerland.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ENOYL REDUCTASE226Thermomyces lanuginosusMutation(s): 0 
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
MALONYL/PALMITOYL TRANSFERASE305Thermomyces lanuginosusMutation(s): 0 
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
KETOACYL SYNTHASE406Thermomyces lanuginosusMutation(s): 0 
UniProt
Find proteins for P0A953 (Escherichia coli (strain K12))
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Go to UniProtKB:  P0A953
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UniProt GroupP0A953
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
KETOACYL REDUCTASE244Thermomyces lanuginosusMutation(s): 0 
UniProt
Find proteins for Q93X62 (Brassica napus)
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UniProt GroupQ93X62
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
DEHYDRATASE248Thermomyces lanuginosusMutation(s): 0 
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Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.20 Å
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 217α = 90
b = 415β = 111.5
c = 222γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
XSCALEdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-03-07
    Type: Initial release
  • Version 1.1: 2024-02-14
    Changes: Data collection, Database references, Refinement description