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- W2971362306 abstract "Crystal Structure of Enoyl-Acyl Carrier Protein Reductase (FabI) proposes a putative inhibitor binding pocket. Table S1. Data collection and refinement statistic. Figure S1. Superimposed protomer structures of AbFabI (green), EcFabI (cyan), SaFabI (purple), and MtFabI (yellow). Upper and lower lips of substrate-binding crevice are shaded with blue and orange ovals. Figure S2. Sequence alignment of AbFabI, EcFabI, SaFabI, and MtFabI. The lower lip (helix α4) of substrate-binding crevice of FabI is shown in orange shade and the upper lip (helices of α9 and α10) of substrate-binding crevice is shown in blue shade. Figure S4. NAD+ binding site. (a) Recognition of NAD+ in AbFabI structure. (b) Comparison of NAD(P)+ bound AbFabI, SaFabI, and MtFabI structures. NAD+–bound AbFabI structure (green), NADP+–bound SaFabI structure (purple), and MtFabI structure (yellow) are superimposed together. Figure S5. GSK625-bound MtFabI structure. NAD+ molecule is shown in green; GSK625 in yellow; hydrophobic residues of upper and lower lips of substrate-binding crevice in orange. Figure S6. Schematic drawing of proposed substrate recognition mechanism of FabIs. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article." @default.
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- W2971362306 date "2019-09-02" @default.
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- W2971362306 title "Crystal Structure of Enoyl‐Acyl Carrier Protein Reductase (FabI) from <i>Acinetobacter baumannii</i> as a Target for Broad‐Spectrum Antibacterial Drug" @default.
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- W2971362306 doi "https://doi.org/10.1002/bkcs.11861" @default.
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