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![[Figure 1]](mh5144fig1mag.jpg)
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Figure 1
Overall structure of H. pylori Csd4. (a) Ribbon diagram of the Csd4-unbound structure. β-Strands, α-helices, 310-helices and loops are shown in cyan, red, yellow and grey, respectively. Three calcium ions are shown as purple spheres. The metal-binding residues in the N-terminal CPase domain are shown as stick models. The blue and black boxes indicate the previously unknown Ca2+-binding sites of the CPase domain and the Ca2+-binding motif of the C-terminal Ig-like domain. The secondary-structure elements were defined by DSSP (Kabsch & Sander, 1983  ). (b) Electrostatic surface diagram of Csd4-unbound. The signal peptide is modelled as a black ribbon diagram. The black and cyan dotted boxes indicate the active-site cleft of the CPase domain and the Ca2+-binding channel of the Ig-like domain. The grey box indicates the highly positively charged surface of the central β-barrel domain. Electrostatic potential at the molecular surface was calculated using APBS (Baker et al., 2001). (c) Ribbon diagram of the Ca2+-binding motif (left) and the surface representation of the Ca2+-bound channel (right) in the Ig-like domain. The OMIT mFo − DFc map (contoured at 10σ) for the calcium ion is coloured green. The Ca2+-binding residues are shown as stick models. The calcium ion and the bound waters are shown as purple and red spheres, respectively. All figures representing the protein structure were drawn using PyMOL (v.1.3r1; Schrödinger). |
![[Figure 1]](mh5144fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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