4fd4
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fd4]] 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=4FD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FD4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4fd4]] 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=4FD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FD4 FirstGlance]. <br> | ||
| - | </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> | + | </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='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'>[https://proteopedia.org/fgij/fg.htm?mol=4fd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fd4 OCA], [https://pdbe.org/4fd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fd4 RCSB], [https://www.ebi.ac.uk/pdbsum/4fd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fd4 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=4fd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fd4 OCA], [https://pdbe.org/4fd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fd4 RCSB], [https://www.ebi.ac.uk/pdbsum/4fd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fd4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q0IFG2_AEDAE Q0IFG2_AEDAE] | [https://www.uniprot.org/uniprot/Q0IFG2_AEDAE Q0IFG2_AEDAE] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4fd4" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of mosquito arylalkylamine N-Acetyltransferase like 5b
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