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Figure 3
3.1 Å resolution map of FAS. (a) Overview of the EM map. The square and circles labelled (B), (C), (D) and (E) indicate the map regions that are enlarged in (b), (c), (d) and (e), respectively. (b) Density at Ser1440 suggesting phosphorylation. (c) Density at residues Cys820 and Cys824 (subunit β) not accounted for by the atomic model. (d) NADPH cofactor density in mesh representation, bound to the active site of the KR domain. Left: the KR active site in the apo form as in the X-ray structure (PDB entry 2uv8; gray) superimposed on our cryoEM structure (green). NADPH and the catalytically active Tyr839 are shown in stick representation. (e) The PPT domain and the dimerization module DM4, which acts as an adaptor to anchor the PPT domain at the perimeter of the FAS barrel (PPT domain in cyan, DM4 in gray and linker helix in yellow; both densities are shown at 1.0σ). Left: the PPT domain traced in the 3.1 Å resolution cryoEM density. Right: the 3.1 Å resolution X-ray map (data from PDB entry 2uv8; Leibundgut et al., 2007BB26) shows that DM4 is well resolved, whereas there is no density for the PPT domain or linker helix.

Volume 7| Part 2| March 2020| Pages 220-227
ISSN: 2052-2525