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Figure 3
Cryo-EM density map and model fitting of the AcrB trimer. (a) Cryo-EM density map of AcrB reconstructed at 2.92 Å resolution, shown from top, side and bottom views. The map reveals clear secondary-structure elements and well resolved transmembrane helices, consistent with the known trimeric architecture. (b) Final atomic model of AcrB fitted into the cryo-EM density map. Each protomer is rendered in a different color to highlight the asymmetric trimer organization. (c) Structural alignment of the final cryo-EM model (blue) with the reference crystal structure (PDB entry 7rr7, yellow), performed using ChimeraX. The r.m.s.d. between the two structures is 1.2 Å. Enlarged views highlight local conformational deviations, including Glu693–Asp711 in protomer B (left) and Ala704–Asp711 in protomer C (right), located within the PN2 subdomain. (d) Close-up view showing the density fit for selected side chains (Trp187 in chain A, Phe572 in chain B, Tyr772 in chain C). The mesh is contoured at 1.6σ in Coot, showing well defined density for aromatic residues.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
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