|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of native arylalkylamine N-Acetyltransferase 2 from the yellow fever mosquito, Aedes aegypti== | | ==Crystal structure of native arylalkylamine N-Acetyltransferase 2 from the yellow fever mosquito, Aedes aegypti== |
| - | <StructureSection load='4fd6' size='340' side='right' caption='[[4fd6]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4fd6' size='340' side='right'caption='[[4fd6]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fd6]] is a 1 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=4FD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FD6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fd6]] is a 1 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=4FD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FD6 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fd4|4fd4]], [[4fd5|4fd5]], [[4fd7|4fd7]]</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]] 1.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AAEL012952, AaeL_AAEL012952 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7159 AEDAE])</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=4fd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fd6 OCA], [https://pdbe.org/4fd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fd6 RCSB], [https://www.ebi.ac.uk/pdbsum/4fd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fd6 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aralkylamine_N-acetyltransferase Aralkylamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.87 2.3.1.87] </span></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=4fd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fd6 OCA], [http://pdbe.org/4fd6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fd6 RCSB], [http://www.ebi.ac.uk/pdbsum/4fd6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fd6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q16KL9_AEDAE Q16KL9_AEDAE] |
| - | Arylalkylamine N-acetyltransferase (aaNAT) catalyzes the transacetylation from acetyl-CoA to arylalkylamines. aaNATs are involved in sclerotization and neurotransmitter inactivation in insects. Phyletic distribution analysis confirms three clusters of aaNAT-like sequences in insects: typical insect aaNAT, polyamine NAT-like aaNAT, and mosquito unique putative aaNAT (paaNAT). Here we studied three proteins: aaNAT2, aaNAT5b, and paaNAT7, each from a different cluster. aaNAT2, a protein from the typical insect aaNAT cluster, uses histamine as a substrate as well as the previously identified arylalkylamines. aaNAT5b, a protein from polyamine NAT -like aaNAT cluster, uses hydrazine and histamine as substrates. The crystal structure of aaNAT2 was determined using single-wavelength anomalous dispersion methods, and that of native aaNAT2, aaNAT5b and paaNAT7 was detected using molecular replacement techniques. All three aaNAT structures have a common fold core of GCN5-related N-acetyltransferase superfamily proteins, along with a unique structural feature: helix/helices between beta3 and beta4 strands. Our data provide a start toward a more comprehensive understanding of the structure-function relationship and physiology of aaNATs from the mosquito Aedes aegypti and serve as a reference for studying the aaNAT family of proteins from other insect species. The structures of three different types of aaNATs may provide targets for designing insecticides for use in mosquito control.
| + | |
| - | | + | |
| - | Evolution of insect arylalkylamine N-acetyltransferases: structural evidence from the yellow fever mosquito, Aedes aegypti.,Han Q, Robinson H, Ding H, Christensen BM, Li J Proc Natl Acad Sci U S A. 2012 Jul 17;109(29):11669-74. doi:, 10.1073/pnas.1206828109. Epub 2012 Jul 2. PMID:22753468<ref>PMID:22753468</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 4fd6" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aedae]] | + | [[Category: Aedes aegypti]] |
| - | [[Category: Aralkylamine N-acetyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Han, Q]] | + | [[Category: Han Q]] |
| - | [[Category: Li, J]] | + | [[Category: Li J]] |
| - | [[Category: Robinson, R]] | + | [[Category: Robinson R]] |
| - | [[Category: Coa binding]]
| + | |
| - | [[Category: Gnat]]
| + | |
| - | [[Category: N-acetyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
