Figure 1
Bacterial AcpS. (a) Multiple sequence alignment of some bacterial AcpS enzymes with known X-ray structures: S. aureus (PDB entry 3f09 ), B. anthracis (PDB entry 3hyk ), B. subtilis (PDB entry 1f7l ), S. pneumoniae (PDB entry 1fth ), V. cholerae (PDB entry 3qmn ) and S. coelicolor (PDB entry 2jbz ). The conserved residues are shaded red and similar residues are displayed in red letters. Residues of the central [beta]-sheet of AcpSSA numbered in (c) are marked with a plus sign. Asterisks indicate residues of AcpSVC that coordinate CoA/K (see Fig. 3[link]c). The coordinators of two magnesium cations, Mg-I and Mg-II (see Figs. 4[link]d and 4[link]e), are shown as I and II, respectively. The green box indicates the Glu-II position, an alternative glutamate of the group II and III PPTs that is involved in coordination of Mg-I. Multiple sequence alignment was performed by ClustalW (available at ) and the figure was generated with ESPript2.2 (Gouet et al., 1999BB28). (b) The quaternary structure of the AcpS enzyme (apo-AcpSSA is shown). (c) The tertiary structure of a single polypeptide of AcpSSA. The residues (in green) of the central [beta]-sheet that are exposed to the interior of AcpS trimer are numbered according to the sequence of AcpSSA. (d) Monomer of AcpSVC with the structurally distinct helix [alpha]6 in dark blue.  [article HTML]