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| | ==Crystal structure of mosquito arylalkylamine N-Acetyltransferase like 5b/spermine N-Acetyltransferase== | | ==Crystal structure of mosquito arylalkylamine N-Acetyltransferase like 5b/spermine N-Acetyltransferase== |
| - | <StructureSection load='5yag' size='340' side='right' caption='[[5yag]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='5yag' size='340' side='right'caption='[[5yag]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5yag]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aedae Aedae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YAG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yag]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aedes_aegypti Aedes aegypti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YAG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">5565529, AAEL004827 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7159 AEDAE])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5yag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yag OCA], [http://pdbe.org/5yag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yag RCSB], [http://www.ebi.ac.uk/pdbsum/5yag PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yag ProSAT]</span></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=5yag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yag OCA], [https://pdbe.org/5yag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yag RCSB], [https://www.ebi.ac.uk/pdbsum/5yag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yag ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q0IFG2_AEDAE Q0IFG2_AEDAE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aedae]] | + | [[Category: Aedes aegypti]] |
| - | [[Category: Guan, H]] | + | [[Category: Large Structures]] |
| - | [[Category: Han, Q]] | + | [[Category: Guan H]] |
| - | [[Category: Li, J]] | + | [[Category: Han Q]] |
| - | [[Category: Robinson, H]] | + | [[Category: Li J]] |
| - | [[Category: Transferase]]
| + | [[Category: Robinson H]] |
| - | [[Category: Transferase complex n-acetyltransferase spermine]]
| + | |
| Structural highlights
Function
Q0IFG2_AEDAE
Publication Abstract from PubMed
Mosquitoes transmit a number of diseases in animals and humans, including Dengue, Chikungunya and Zika viruses that affect millions of people each year. Controlling the disease-transmitting mosquitoes has proven to be a successful strategy to reduce the viruses transmission. Polyamines are required for the life cycle of the RNA viruses, Chikungunya virus and Zika virus, and a depletion of spermidine and spermine in the host via induction of spermine N-acetyltransferase restricts their replication. Spermine N-acetyltransferase is a key catabolic enzyme in the polyamine pathway, however there is no information of the enzyme identification in any insects. Aliphatic polyamines play a fundamental role in tissue growth and development in organisms. They are acetylated by spermidine/spermine N1-acetyltransferase (SAT). In this study we provided a molecular and biochemical identification of SAT from Aedes aegypti mosquitoes. Screening of purified recombinant proteins against polyamines established that aaNAT5b, named previously based on sequence similarity with identified aaNAT1 in insects, is active to spermine and spermidine. A crystal structure was determined and used in molecular docking in this study. Key residues were identified to be involved in spermine binding using molecular docking and simulation. In addition, SAT transcript was down regulated by blood feeding using a real time PCR test. Based on its substrate profile and transcriptional levels after blood feeding, together with previous reports for polyamines required in arboviruses replication, SAT might be potentially used as a target to control arboviruses with human interference.
Identification of aaNAT5b as a spermine N-acetyltransferase in the mosquito, Aedes aegypti.,Guan H, Wang M, Liao C, Liang J, Mehere P, Tian M, Liu H, Robinson H, Li J, Han Q PLoS One. 2018 Mar 19;13(3):e0194499. doi: 10.1371/journal.pone.0194499., eCollection 2018. PMID:29554129[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guan H, Wang M, Liao C, Liang J, Mehere P, Tian M, Liu H, Robinson H, Li J, Han Q. Identification of aaNAT5b as a spermine N-acetyltransferase in the mosquito, Aedes aegypti. PLoS One. 2018 Mar 19;13(3):e0194499. doi: 10.1371/journal.pone.0194499., eCollection 2018. PMID:29554129 doi:http://dx.doi.org/10.1371/journal.pone.0194499
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