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. 2017 Feb 28;53(18):2772-2775.
doi: 10.1039/c7cc00783c.

X-ray crystallographic structure of a teixobactin analogue reveals key interactions of the teixobactin pharmacophore

H Yang  1 , D R Du Bois  1 , J W Ziller  1 , J S Nowick  1
Affiliations

X-ray crystallographic structure of a teixobactin analogue reveals key interactions of the teixobactin pharmacophore

H Yang et al. Chem Commun (Camb). .

Abstract

The X-ray crystallographic structure of a truncated teixobactin analogue reveals hydrogen-bonding and hydrophobic interactions and a cavity that binds a chloride anion. Minimum inhibitory concentration (MIC) assays against Gram-positive bacteria correlate the observed structure with antibiotic activity.

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Figures

Fig. 1
Fig. 1
Structures of teixobactin and homologues.
Fig. 2
Fig. 2
X-ray crystallographic structure of Ac-Δ1–5-Arg10-teixobactin as the hydrochloride salt. (A) Top view. (B) Side view. (C) Rotated side view, in which the side chains of Ile6 and Ile11 are shown as spheres. Hydrogens attached to carbons that are shown as sticks are omitted for clarity. Water of crystallization (1.5 H2O per molecule of peptide) is not shown.
Fig. 3
Fig. 3
Summary of key findings.
See this image and copyright information in PMC

References

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