Dimerization of inositol monophosphatase SuhB is not constitutive, but induced by binding of the activator Mg-4

<p><b>Copyright information:</b></p><p>Taken from "Dimerization of inositol monophosphatase SuhB is not constitutive, but induced by binding of the activator Mg"</p><p>http://www.biomedcentral.com/1472-6807/7/55</p><p>BMC Structural Biology 2007;7():55-55.</p><p>Published online 28 Aug 2007</p><p>PMCID:PMC2080633.</p><p></p>uhB was at 1.0 mg.mlin 20 mM Tris-HCl pH 7.9, 50 mM NaCl, plus MgClor LiCl as indicated. Samples were centrifuged at 40,000 rpm at 4°C for at least 12 hours. The peak at 1.6 corresponds to a molecular weight of 30,147 Da, the peak at 2.5 corresponds to 50,116 Da

Dimerization of inositol monophosphatase SuhB is not constitutive, but induced by binding of the activator Mg-5

<p><b>Copyright information:</b></p><p>Taken from "Dimerization of inositol monophosphatase SuhB is not constitutive, but induced by binding of the activator Mg"</p><p>http://www.biomedcentral.com/1472-6807/7/55</p><p>BMC Structural Biology 2007;7():55-55.</p><p>Published online 28 Aug 2007</p><p>PMCID:PMC2080633.</p><p></p>a-layered αβαβα-sandwich arrangement of IMPases (cf. Figure 1). () Dimer of SuhB formed by subunits A (blue, yellow) and C (lightblue, green). Selected secondary structure elements are labelled for ease of comparison with panel A. Grey spheres indicate boundaries of disordered loops, with corresponding residue numbers in black type. A (modelled) molecule of inositol-1-phosphate in ball-and-stick representation indicates the location of the active site(s) in both panels

Dimerization of inositol monophosphatase SuhB is not constitutive, but induced by binding of the activator Mg-0

<p><b>Copyright information:</b></p><p>Taken from "Dimerization of inositol monophosphatase SuhB is not constitutive, but induced by binding of the activator Mg"</p><p>http://www.biomedcentral.com/1472-6807/7/55</p><p>BMC Structural Biology 2007;7():55-55.</p><p>Published online 28 Aug 2007</p><p>PMCID:PMC2080633.</p><p></p>a-layered αβαβα-sandwich arrangement of IMPases (cf. Figure 1). () Dimer of SuhB formed by subunits A (blue, yellow) and C (lightblue, green). Selected secondary structure elements are labelled for ease of comparison with panel A. Grey spheres indicate boundaries of disordered loops, with corresponding residue numbers in black type. A (modelled) molecule of inositol-1-phosphate in ball-and-stick representation indicates the location of the active site(s) in both panels

Dimerization of inositol monophosphatase SuhB is not constitutive, but induced by binding of the activator Mg-1

<p><b>Copyright information:</b></p><p>Taken from "Dimerization of inositol monophosphatase SuhB is not constitutive, but induced by binding of the activator Mg"</p><p>http://www.biomedcentral.com/1472-6807/7/55</p><p>BMC Structural Biology 2007;7():55-55.</p><p>Published online 28 Aug 2007</p><p>PMCID:PMC2080633.</p><p></p> carbons in light grey) modelled based on superimposition with the structures of bovine (PDB:, [17]) and human IMPase (PDB:, [29]). Residues in contact with metal sites and substrate in the modelled complex are shown as sticks and numbered according to the SuhB sequence. Secondary structure elements are coloured as in Figure 2A. The loop in violet indicates the approximate position of the α1-α2 loop, based on the superposition with PDB: [29]. () Bias-free difference density map of the β9-α6 loop in SuhB, calculated after simulated annealing of the model with residues 178–188 deleted and contoured at 2σ. The density is superimposed with SuhB (blue sticks) and human IMPase in complex with inositol-1-phosphate (light green, PDB:, [29]). Putative (grey) and experimental (red) contact distances with substrate are indicated. () Active site of subunit C of SuhB with σ-weighted Fo-Fc map contoured at 3σ, showing unexplained density around the putative substrate position and metal site 1

Dimerization of inositol monophosphatase SuhB is not constitutive, but induced by binding of the activator Mg-2

<p><b>Copyright information:</b></p><p>Taken from "Dimerization of inositol monophosphatase SuhB is not constitutive, but induced by binding of the activator Mg"</p><p>http://www.biomedcentral.com/1472-6807/7/55</p><p>BMC Structural Biology 2007;7():55-55.</p><p>Published online 28 Aug 2007</p><p>PMCID:PMC2080633.</p><p></p>e matching. The spacing of the helix axes is indicated in units of Å and the black oval indicates the position of the non-crystallographic 2-fold axis mapping the subunits onto each other. () The helix α6 interface in with side chains contributing to the contact surface indicated as sticks in cyan (subunit A) and yellow (subunit C). () Contact surface (magenta) of subunit A calculated and visualised using Swiss PDB Viewer [50]. The active site indicated by a molecule of inositol-1-phosphate (yellow sticks)

Supplementary information files for The adaptability of the ion binding site by the Ag(I)/Cu(I) periplasmic chaperone SilF.

Supplementary files for article The adaptability of the ion binding site by the Ag(I)/Cu(I) periplasmic chaperone SilF.The periplasmic chaperone SilF has been identified as part of an Ag(I) detoxification system in Gram negative bacteria. Sil proteins also bind Cu(I), but with reported weaker affinity, therefore leading to the designation of a specific detoxification system for Ag(I). Using isothermal titration calorimetry we show that binding of both ions is not only tighter than previously thought, but of very similar affinities. We investigated the structural origins of ion binding using molecular dynamics and QM/MM simulations underpinned by structural and biophysical experiments. The results of this analysis showed that the binding site adapts to accommodate either ion, with key interactions with the solvent in the case of Cu(I). The implications of this are that Gram negative bacteria do not appear to have evolved a specific Ag(I) efflux system but take advantage of the existing Cu(I) detoxification system. Therefore, there are consequences for how we define a particular metal resistance mechanism and understand its evolution in the environment.</p