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The | ==Crystal structure of Nucleoside Diphosphate Kinase from Schistosoma mansoni in complex with ADP== | ||
<StructureSection load='5kk8' size='340' side='right'caption='[[5kk8]], [[Resolution|resolution]] 2.11Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5kk8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KK8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KK8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.11Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5kk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kk8 OCA], [https://pdbe.org/5kk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kk8 RCSB], [https://www.ebi.ac.uk/pdbsum/5kk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kk8 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nucleoside diphosphate kinases (NDPKs) are crucial to keep the high triphosphate nucleotide levels in the biological process. The enzymatic mechanism has been extensively described; however, the structural characteristics and kinetic parameters have never been fully determined. In Schistosoma mansoni, NDPK (SmNDPK) is directly involved in the pyrimidine and purine salvage pathways, being essential for nucleotide metabolism. The SmNDPK enzymatic activity is the highest of the known purine metabolisms when compared to the mammalian NDPKs, suggesting the importance of this enzyme in the worm metabolism. Here, we report the recombinant expression of SmNDPK that resulted in 1.7 and 1.9 A apo-form structure in different space-groups, as well as the 2.1 A SmNDPK.ADP complex. The binding and kinetic assays reveal the ATP-dependence for enzyme activation. Moreover, in situ hybridization showed that SmNDPK transcripts are found in reproductive organs and in the esophagus gland of adult worms, which can be intrinsically related with the oviposition and digestive processes. These results will help us fully understand the crucial participation of this enzyme in Schistosoma mansoni and its importance for the pathology of the disease. | |||
Characterization of a Schistosoma mansoni NDPK expressed in sexual and digestive organs.,Torini JR, de Freitas Fernandes A, Balasco Serrao VH, Romanello L, Bird LE, Nettleship JE, Owens RJ, Brandao-Neto J, Zeraik AE, DeMarco R, D'Muniz Pereira H Mol Biochem Parasitol. 2019 May 16;231:111187. doi:, 10.1016/j.molbiopara.2019.111187. PMID:31103556<ref>PMID:31103556</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5kk8" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Brandao-Neto | ==See Also== | ||
[[Category: | *[[Nucleoside diphosphate kinase 3D structures|Nucleoside diphosphate kinase 3D structures]] | ||
[[Category: Nettleship | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Schistosoma mansoni]] | |||
[[Category: Aller P]] | |||
[[Category: Bird LE]] | |||
[[Category: Brandao-Neto J]] | |||
[[Category: DeMarco R]] | |||
[[Category: Nettleship JE]] | |||
[[Category: Owens RJ]] | |||
[[Category: Pereira HM]] | |||
[[Category: Romanello L]] | |||
[[Category: Torini JRS]] |
Latest revision as of 13:02, 27 September 2023
Crystal structure of Nucleoside Diphosphate Kinase from Schistosoma mansoni in complex with ADPCrystal structure of Nucleoside Diphosphate Kinase from Schistosoma mansoni in complex with ADP
Structural highlights
Publication Abstract from PubMedNucleoside diphosphate kinases (NDPKs) are crucial to keep the high triphosphate nucleotide levels in the biological process. The enzymatic mechanism has been extensively described; however, the structural characteristics and kinetic parameters have never been fully determined. In Schistosoma mansoni, NDPK (SmNDPK) is directly involved in the pyrimidine and purine salvage pathways, being essential for nucleotide metabolism. The SmNDPK enzymatic activity is the highest of the known purine metabolisms when compared to the mammalian NDPKs, suggesting the importance of this enzyme in the worm metabolism. Here, we report the recombinant expression of SmNDPK that resulted in 1.7 and 1.9 A apo-form structure in different space-groups, as well as the 2.1 A SmNDPK.ADP complex. The binding and kinetic assays reveal the ATP-dependence for enzyme activation. Moreover, in situ hybridization showed that SmNDPK transcripts are found in reproductive organs and in the esophagus gland of adult worms, which can be intrinsically related with the oviposition and digestive processes. These results will help us fully understand the crucial participation of this enzyme in Schistosoma mansoni and its importance for the pathology of the disease. Characterization of a Schistosoma mansoni NDPK expressed in sexual and digestive organs.,Torini JR, de Freitas Fernandes A, Balasco Serrao VH, Romanello L, Bird LE, Nettleship JE, Owens RJ, Brandao-Neto J, Zeraik AE, DeMarco R, D'Muniz Pereira H Mol Biochem Parasitol. 2019 May 16;231:111187. doi:, 10.1016/j.molbiopara.2019.111187. PMID:31103556[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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