Structures of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei

Edwards, T.E.; Leibly, D.J.; Bhandari, J.; Statnekov, J.B.; Phan, I.; Dieterich, S.H.; Abendroth, J.; Staker, B.L.; Van Voorhis, W.C.; Myler, P.J.; Stewart, L.J.

doi:10.1107/S1744309111004349

Acta Crystallographica Section F
Acta Crystallographica
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Figure 3
Crystal structure of Bp PPAT solved at 1.6 Å resolution. (a) Monomeric structure of Bp PPAT in ribbon format with molecular-surface rendering in light transparency. Active-site components are modelled in stick representation and selected waters are shown as spheres. The active-site ligand-omit density map (|F_o| − |F_c|) is shown as a green mesh contoured at 3.0σ. (b) Close-up of the active site. The final protein model is shown in ribbon representation along with 4′-diphosphopantetheine, adenine and a sulfate ion in stick representation and selected waters as red spheres. The active-site ligand-omit electron-density map (|F_o| − |F_c|) is shown as a green mesh contoured at 3.0σ. (c) Active site as in (b) with the 2|F_o| − |F_c| electron-density map shown as a blue mesh contoured at 1.0σ. (d) Overlay of the final refined structure of Bp PPAT from (c) along with the structure of Bp PPAT-bound dephospho-coenzyme A solved at 2.1 Å resolution with coloring as in Fig. 2

(b).

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ISSN: 2053-230X

Volume 67| Part 9| August 2011| Pages 1032-1037

doi:10.1107/S1744309111004349

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