Donor substrate recognition in the raffinose-bound E342A mutant of fructosyltransferase levansucrase-1

(pale red). () Superposition of sucrose-bound (1PT2, [11], light blue) and raffinose-bound E342A (this study). Dashed lines in cyan indicate H-bond interactions conserved between both complexes, those in red indicate additional contacts made by the galactosyl moiety.<p><b>Copyright information:</b></p><p>Taken from "Donor substrate recognition in the raffinose-bound E342A mutant of fructosyltransferase levansucrase"</p><p>http://www.biomedcentral.com/1472-6807/8/16</p><p>BMC Structural Biology 2008;8():16-16.</p><p>Published online 17 Mar 2008</p><p>PMCID:PMC2277421.</p><p></p

Donor substrate recognition in the raffinose-bound E342A mutant of fructosyltransferase levansucrase-2

indicated by dashed green lines. Residues making van der Waals or hydrophobic contacts are indicated by the 'bent comb' symbol. Water molecules appear as spheres in light blue, carbon, oxygen and nitrogen are in black, red and dark blue, respectively.<p><b>Copyright information:</b></p><p>Taken from "Donor substrate recognition in the raffinose-bound E342A mutant of fructosyltransferase levansucrase"</p><p>http://www.biomedcentral.com/1472-6807/8/16</p><p>BMC Structural Biology 2008;8():16-16.</p><p>Published online 17 Mar 2008</p><p>PMCID:PMC2277421.</p><p></p

Donor substrate recognition in the raffinose-bound E342A mutant of fructosyltransferase levansucrase-0

Rived from the wild-type enzyme structure (1OYG, [11]). The maps (2.1 Å resolution) are contoured at 5σ (panels -) or 4σ (panel ), with positive and negative density in blue and red, respectively. The stick models are colour-coded by carbon atoms as follows: wild type enzyme (green), D86A (magenta – panel , D247A (yellow – panel , E342A (grey – panel ) and raffinose-bound E342A (pale red – panel ).<p><b>Copyright information:</b></p><p>Taken from "Donor substrate recognition in the raffinose-bound E342A mutant of fructosyltransferase levansucrase"</p><p>http://www.biomedcentral.com/1472-6807/8/16</p><p>BMC Structural Biology 2008;8():16-16.</p><p>Published online 17 Mar 2008</p><p>PMCID:PMC2277421.</p><p></p

Replacement of the essential Arp2 gene by its homologue using parasexual genetics-3

<p><b>Copyright information:</b></p><p>Taken from "Replacement of the essential Arp2 gene by its homologue using parasexual genetics"</p><p>http://www.biomedcentral.com/1471-2156/8/28</p><p>BMC Genetics 2007;8():28-28.</p><p>Published online 6 Jun 2007</p><p>PMCID:PMC1904233.</p><p></p>alysed by SDS-PAGE and western blotting as described in Materials and Methods. Cell lysates (L) and immunoprecipitates (IP) from three cell types were examined; AX3 (wild type), MZ10 (haploid rescued with -tagged Arp2 replacement), MZ11 (haploid rescued with -tagged Arp2 replacement). Blots were probed with antibodies to Arp2, Arp3 and the p21-arc subunits

Replacement of the essential Arp2 gene by its homologue using parasexual genetics-2

<p><b>Copyright information:</b></p><p>Taken from "Replacement of the essential Arp2 gene by its homologue using parasexual genetics"</p><p>http://www.biomedcentral.com/1471-2156/8/28</p><p>BMC Genetics 2007;8():28-28.</p><p>Published online 6 Jun 2007</p><p>PMCID:PMC1904233.</p><p></p>) Cell lysates prepared from equal numbers of cells were separated by SDS-PAGE, transferred onto nitrocellulose and immunoblotted as described in Materials and Methods. Blots were probed with anti-Arp2 antibody. (ii) 20 μg of total protein was separated by SDS-PAGE, transferred onto PVDF and immunoblotted as described in Materials and Methods. Blots were probed with anti-Arp2 and mAb 9E10 anti-antibodies. All results are representative two to three experiments. . Under-agar migratory response of cells to a gradient of folate. Arrows indicate the direction of cell migration (increasing folate concentration); Scale bar is 50 μm. Scale bar is 10 μm. Response of cells spotted on nitrocellulose filters, to a lateral light source (48 hrs). The light source is always to the right of the image. Arrows indicate the direction of migration; Scale bar is 5 mm. Scale bar is 1 mm. Fruiting body morphology of cells after development on nitrocellulose filters (48 hrs). Scale bar is 1 mm. Scale bar is 0.1 mm

Replacement of the essential Arp2 gene by its homologue using parasexual genetics-0

<p><b>Copyright information:</b></p><p>Taken from "Replacement of the essential Arp2 gene by its homologue using parasexual genetics"</p><p>http://www.biomedcentral.com/1471-2156/8/28</p><p>BMC Genetics 2007;8():28-28.</p><p>Published online 6 Jun 2007</p><p>PMCID:PMC1904233.</p><p></p>esidues and residues present in any one specie. Light shading represents conserved residues. Dashes are incorporated to optimise alignment. Comparison of Arp2 with the human, and homologues. Numbers in () show percent identity (the proportion of identical amino acids over the full length of the aligned proteins expressed as a percentage). Numbers in [] show percent similarity (the proportion of both identical and conserved amino acids over the full length of the aligned proteins expressed as a percentage). Key features of Arp2 from and based on respective GenBank entries

Replacement of the essential Arp2 gene by its homologue using parasexual genetics-4

<p><b>Copyright information:</b></p><p>Taken from "Replacement of the essential Arp2 gene by its homologue using parasexual genetics"</p><p>http://www.biomedcentral.com/1471-2156/8/28</p><p>BMC Genetics 2007;8():28-28.</p><p>Published online 6 Jun 2007</p><p>PMCID:PMC1904233.</p><p></p>esidues and residues present in any one specie. Light shading represents conserved residues. Dashes are incorporated to optimise alignment. Comparison of Arp2 with the human, and homologues. Numbers in () show percent identity (the proportion of identical amino acids over the full length of the aligned proteins expressed as a percentage). Numbers in [] show percent similarity (the proportion of both identical and conserved amino acids over the full length of the aligned proteins expressed as a percentage). Key features of Arp2 from and based on respective GenBank entries

Replacement of the essential Arp2 gene by its homologue using parasexual genetics-1

<p><b>Copyright information:</b></p><p>Taken from "Replacement of the essential Arp2 gene by its homologue using parasexual genetics"</p><p>http://www.biomedcentral.com/1471-2156/8/28</p><p>BMC Genetics 2007;8():28-28.</p><p>Published online 6 Jun 2007</p><p>PMCID:PMC1904233.</p><p></p>he gene replacement method. Western hybridisation screen for the gene replacement method. Banding patterns seen with anti-Arp2 and mAb 9E10 anti-antibody are shown. Lane 1 shows the pattern seen for strains DH1, JH10, DIR1 and DJK45; lane 2 shows the pattern seen for strains DMZ10 and DMZ11; lane 3 shows the pattern for a haploid strain containing both wild-type and -tagged Arp2; lane 4 shows the pattern of the replacement strains MZ10 and MZ11

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-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