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PDBsum entry 2uva

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Transferase PDB id
2uva
Jmol
Contents
Protein chains
(+ 0 more) 2060 a.a.
Ligands
FMN ×6

References listed in PDB file
Key reference
Title Structure of fungal fatty acid synthase and implications for iterative substrate shuttling.
Authors S.Jenni, M.Leibundgut, D.Boehringer, C.Frick, B.Mikolásek, N.Ban.
Ref. Science, 2007, 316, 254-261. [DOI no: 10.1126/science.1138248]
PubMed id 17431175
Abstract
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.
Figure 1.
Fig. 1. Structure of the fungal FAS. (A) A ribbon representation of the refined T. lanuginosus FAS structure is shown in two side views along the two-fold axis of symmetry (left and middle) and in a top view along the three-fold axis of symmetry (right). Helices belonging to the central wheel are colored red, helices of the capping domes are shown in green, ß strands are colored blue. The particle has an approximate height and width of 270 Å by 250 Å. "Windows" in the side walls and at the top of the particle are labeled as openings 1 to 5, connections between the dome and the central disk as C1, C2, and C3. (B) Quaternary structure and subunit distribution of the FAS complex. The heterododecameric complex is composed of a D[3]-symmetrical [6] hexamer (subunits are colored pink and blue) and two C[3]-symmetrical ß[3] trimers (subunits are colored green, yellow and gray). In the side view (left), the ß[3] trimers have been moved away from the chains as indicated by the arrows.
Figure 6.
Fig. 6. Substrate shuttling in the fungal FAS. (A) On the basis of the shortest distances between both ACP anchor points (green) and all catalytic domains in the reaction chamber, acompleteset of catalytic sites necessary for the cyclic reaction can be defined (red). On accountofthe elasticity of linkers (yellow), free diffusion of ACP (cyan) would be "channeled" into a circular path, which further increases the local concentration of the ACP in the area where active sites are distributed (arrow). (B) The reaction chamber contains three complete sets of active sites, which are arranged in an approximate plane around the peripheral ACP anchors. Note that different (pink, blue) and ß chains (green, yellow, gray) contribute to each catalytic set.
The above figures are reprinted by permission from the AAAs: Science (2007, 316, 254-261) copyright 2007.
PROCHECK
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