Different binding modes of bases in the main part of BBS residues, showing stick model for residues S118 and 229–232.

<p><b>A</b>. H-bond scheme for adenine in the BBS of wild-type <i>Sm</i>MTAP. <b>B</b>. adenine in S12T/N87T chain B. D230 does not form direct interaction with the base. <b>C</b>. In S12T chain C the orientation of D230 is also different. <b>D</b>. Tubercidin in wild-type <i>Sm</i>MTAP, the side chain of D230 points away to active site. <b>E</b>. In Q289L Tubercidin chain A D230 form canonical contacts within the base even being 7-deaza-adenosine. <b>F</b>. MTA molecule in S12Tmutant active site. The active site shows high conformational plasticity especially for the side chain of D230 residue.</p

Ligplus⁺ diagrams for ligands in the <i>Sm</i>MTAP active site.

<p>A. adenine; B. tubercidin; C., different binding modes of tubercidin in the active site interacting with both D230 and Q289 residues. D. MTA.</p

Data collection, processing and refinement statistics.

<p>Data collection, processing and refinement statistics.</p

Part of the phosphate and ribose binding sites showing the interactions between the side chain of Q289 and both S12 and O5' of tubercidin.

<p>Human enzymes possess leucine in this position and thus do not form these interactions.</p

Sequence alignment of MTAPs from <i>S</i>. <i>mansoni</i> (<i>Sm</i>MTAP), <i>S. japonicum</i> (<i>Sj</i>MTAP) and human (<i>Hs</i>MTAP).

<p><i>Sm</i>MTAP shares 77% and 47% identity with <i>Sj</i>MTAP and <i>Hs</i>MTAP, respectively. The <i>Sm</i>MTAP secondary structure elements are labeled and shown as arrows and helices. One sequence insertion also present in both <i>Schistosoma</i> species could be observed between beta strands 10 and 11.</p

Ligplus⁺ plots for the sulphate molecule.

<p><b>A</b>. wt <i>Sm</i>MTAP. <b>B</b>. Double mutant S12T/N87T and their consequence in sulphate/phosphate binding, where 3 new H-bonds are formed.</p

Crystal Structure of <i>Schistosoma mansoni</i> Adenosine Phosphorylase/5’-Methylthioadenosine Phosphorylase and Its Importance on Adenosine Salvage Pathway - Fig 4

<p>A. Composite omit map contoured at 1σ for the region containing the SS bond in <i>Sm</i>MTAP. B. Stick model for the same region showed in A. This disulphide bond is formed by the residues Cys 233 and Cys 242 only in some Apo mutant structures. This SS bond helps maintain the gate loop in open conformation and could be involved in the nucleoside accessibility of the active site.</p

Stereo image of gate loop movement between adenine complex structure (red) and APO (blue).

<p>The D230 main residue in the active site is shown in yellow. The movement involves residues 229–253. In the APO structure, D230 points away from the active site. The presence of the base or base moiety in the base bind site appears to be necessary to "close" the gate loop in the base interacting conformation.</p

Analysis of genes shared with Deuterostomia and with possible roles in host interactions-3

<p><b>Copyright information:</b></p><p>Taken from "Analysis of genes shared with Deuterostomia and with possible roles in host interactions"</p><p>http://www.biomedcentral.com/1471-2164/8/407</p><p>BMC Genomics 2007;8():407-407.</p><p>Published online 8 Nov 2007</p><p>PMCID:PMC2194728.</p><p></p>Maximum Likelihood tree constructed from the alignment of SmVASLv6a and other vasohibins found in public databases. The branch is represented in red. Numbers next to the branches represent bootstrap values (in 1000 samplings). : Real time RT-PCR using total RNA samples from egg, miracidium, cercaria, schistosomulum or adult and primers for SmVASL. Relative fold change was calculated by comparing the Ct value for each sample to Ct values for alpha-tubulin (internal standard)

Analysis of genes shared with Deuterostomia and with possible roles in host interactions-2

<p><b>Copyright information:</b></p><p>Taken from "Analysis of genes shared with Deuterostomia and with possible roles in host interactions"</p><p>http://www.biomedcentral.com/1471-2164/8/407</p><p>BMC Genomics 2007;8():407-407.</p><p>Published online 8 Nov 2007</p><p>PMCID:PMC2194728.</p><p></p>ck gray bar at the top represents the genomic sequence of Supercontig_0000046. Coding sequences, UTRs and introns are represented by thick, thin and dashed lines, respectively. We have colored and numbered the different exons consecutively in an arbitrary way, in the order that each new exon splicing form appears in Figure 4A. Primers that were used for the RT-PCR amplification and RACE experiments of SmVASL alternatively spliced forms are represented by green and blue arrows, respectively. Deduced protein-coding ORFs of SmVASL message are represented by thick colored lines, and the lengths of the deduced encoded proteins are displayed at the right side of each splice variant. The asterisks next to SmVASLv6, SmVASLv6a and SmVASLv6b indicate that the latter two are the result of a 3'-RACE-PCR experiment (3'-RACE primers represented by blue arrows); : Local alignment (BLAST) showing the conserved region of SmVASLv6a and human vasohibin 2; : Agarose gel electrophoresis of RT-PCR products from a reaction performed with primers indicated in panel A with green arrows. indicates that cDNA was synthesized by Reverse Transcriptase with poly-dT priming using RNA as template, and PCR was subsequently performed. indicates a negative control where PCR was performed with an RNA sample incubated with poly-dT but no reverse transcriptase, to control for the absence of genomic DNA contamination