PDBsum entry 2pff

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Transferase PDB id
Protein chains
1683 a.a.
2006 a.a.
65 a.a.

References listed in PDB file
Key reference
Title The crystal structure of yeast fatty acid synthase, A cellular machine with eight active sites working together.
Authors I.B.Lomakin, Y.Xiong, T.A.Steitz.
Ref. Cell, 2007, 129, 319-332. [DOI no: 10.1016/j.cell.2007.03.013]
PubMed id 17448991
In yeast, the whole metabolic pathway for making 16- and 18-carbon fatty acids is carried out by fatty acid synthase, a 2.6 megadalton molecular-weight macromolecular assembly containing six copies of all eight catalytic centers. We have determined its crystal structure, which illuminates how this enzyme is initially activated and then carries out multiple steps of synthesis in each of six sterically isolated reaction chambers. Six of the catalytic sites are in the wall of the assembly facing an acyl carrier protein (ACP) bound to the ketoacyl synthase domain. Two-dimensional diffusion of substrates to the catalytic sites may be achieved by the electrostatically negative ACP swinging to each of the six electrostatically positive catalytic sites. The phosphopantetheinyl transferase domain lies outside the shell of the assembly, inaccessible to ACP that lies inside, suggesting that the attachment of the pantetheine arm to ACP must occur before complete assembly of the complex.
Figure 4.
Figure 4. Structure of the β Subunit
(A) Domain organization of the β subunit is shown at the top, a ribbon diagram of the FAS particle without the α subunits on the left, and an individual β subunit on the right.
(B, C, E, and F) Ribbon diagrams of individual domains. Red sticks show side chains of active-site residues.
(B) AT (green), AT helical flap (blue).
(C) MPT (beige), MPT helical flap (blue). The orientation is the same as that of AT.
(D) Composition of the AT active center (pale green). Residues involved in catalysis are shown in red. Malonate (yellow) is modeled into the putative active sites as a reference (from PDB ID code 2G2Z).
(E) ER (blue) with the FMN molecule (green) in the active site.
(F) DHn (light blue) and DHc (cyan) form a pseudodimer (DH domain).
Figure 6.
Figure 6. ACP Interactions with Electrostatically Complementary Active Sites
(A) Surface electrostatic potential representations (blue for positive charge, red for negative charge) shown for KR (top left), AT (top center), MPT (top right), KS/KS dimer (bottom left), and ACP (bottom center). Active centers are shown in yellow.
(B) Surface representation of the α subunit domain 1 (ACP subdomain in gray-green, C-terminal helical subdomain in green) bound to the KS/KS dimer (blue) and the “hub” (pink).
The above figures are reprinted by permission from Cell Press: Cell (2007, 129, 319-332) copyright 2007.
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