2UV9: Crystal Structure Of Fatty Acid Synthase From Thermomyces Lanuginosus At 3.1 Angstrom Resolution

We report crystal structures of the 2.6-megadalton alpha6beta6 heterododecameric fatty acid synthase from Thermomyces lanuginosus at 3.1 angstrom resolution. The alpha and beta polypeptide chains form the six catalytic domains required for fatty acid synthesis and numerous expansion segments responsible for extensive intersubunit connections. Detailed views of all active sites provide insights into substrate specificities and catalytic mechanisms and reveal their unique characteristics, which are due to the integration into the multienzyme. The mode of acyl carrier protein attachment in the reaction chamber, together with the spatial distribution of active sites, suggests that iterative substrate shuttling is achieved by a relatively restricted circular motion of the carrier domain in the multifunctional enzyme.
MMDB ID: 99307
PDB Deposition Date: 2007/3/9
Updated in MMDB: 2012/08
Experimental Method:
x-ray diffraction
Resolution: 3.1  Å
Source Organism:
Similar Structures:
Merged PDB IDs:2UV9 2UVA
Asymmetric Unit for 2UV9: dodecameric
Molecular Components in 2UV9
Label Count Molecule
Proteins (12 molecules)
Fatty Acid Synthase Alpha Subunits
Molecule annotation
Fatty Acid Synthase Beta Subunits
Molecule annotation
Chemicals (6 molecules)
Molecule information is not avaliable.
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Citing MMDB