1. Volume 20, Issue 6, Pages 1107-1117 (June 2012)
Screening and In Situ Synthesis Using Crystals of a NAD Kinase Lead to a Potent Antistaphylococcal Compound 
Muriel Gelin, Guillaume Poncet-Montange, Liliane Assairi, Laurence Morellato, Valérie Huteau, Laurence Dugué, Olivier Dussurget, Sylvie Pochet, Gilles Labesse 
Structure 
Volume 20, Issue 6, Pages (June 2012)
DOI: /j.str
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2. Structure 2012 20, 1107-1117DOI: (10.1016/j.str.2012.03.024)
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3. Figure 1 Structures of Molecules 1–15 Used in This Study
Picture drawn with the software Chemdraw.
Structure  , DOI: ( /j.str )
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4. Figure 2 In Cristallo Screening
Crystal structures of adenosine derivatives bound to LmNADK1 active site: (A) MTA (1), (B) 5′-O-propargyl-5′-deoxyadenosine (4), and (C) 5′-azido-5′-deoxyadenosine (6). In all cases, two ligands occupy the active site. Views of the 2Fo−Fc electron density map in the active site with the ligand molecule omitted in the Fourier synthesis. Map is contoured at 1.0 σ. The picture (and Figures 3 and 4) was generated by the program PYMOL (
Structure  , DOI: ( /j.str )
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5. Figure 3 In Situ Amidation
Crystal structures of LmNADK1 active site in complex with products of in situ chemistry detected in the wild-type enzyme or the unreacted precursors observed in the mutant LmNADK1-H223E. (A) 8-bromo-5′-amino-5′-deoxyadenosine (9) with covalently linked citrate in subsite N or unreacted in subsite A, (B) 8-bromo-5′-amino-5′-deoxyadenosine (9) covalently linked in situ with 8-thioglycolic-5′-azido-5′-deoxyadenosine (10), and (C) 8-bromo-5′-amino-5′-deoxyadenosine (9) unreacted after soaking in the crystals of the mutated LmNADK1-H223E.
Structure  , DOI: ( /j.str )
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6. Figure 4 Crystal Structure Comparison and Catalytic Mechanism
Structural comparison of 2′-phospho-AppA bound to LmNADK1 (PDB 2i2e; shown as sticks with green carbons) and the amidation product formed in situ (this study; shown as sticks with gray carbons). For clarity, only the side chain of the two catalytic residues is indicated. The side chain of histidine H223 is hydrogen bonded to a phosphate group of the diphosphate-diadenosine, a substrate mimic of NAD kinases. Distances (in angstroms) are shown in violet (crystal structure of LmNADK1-2′-phosphoAppA) and dark blue (combined model of the conformation of H223 to catalyze amide bond formation).
Structure  , DOI: ( /j.str )
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7. Figure 5 Antibacterial Effect of NADK Inhibitor on S. aureus
Suspensions (100 μl) of S. aureus corresponding to bacteria were incubated overnight at 37°C with increasing concentrations of inhibitor (1 to 100 μg/ml). Percent bacterial killing was determined as the ratio of colony-forming units after incubation with inhibitor to that of colony-forming units after incubation with buffer alone. Data are mean values ± SD from three separate experiments. ∗p < 0.05, Student's t test.
Structure  , DOI: ( /j.str )
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