4FD6
Crystal structure of native arylalkylamine N-Acetyltransferase 2 from the yellow fever mosquito, Aedes aegypti
Summary for 4FD6
| Entry DOI | 10.2210/pdb4fd6/pdb |
| Related | 4FD4 4FD5 4FD7 |
| Descriptor | arylalkylamine N-Acetyltransferase 2 (2 entities in total) |
| Functional Keywords | gnat, n-acetyltransferase, coa binding, transferase |
| Biological source | Aedes aegypti (Yellowfever mosquito) |
| Total number of polymer chains | 1 |
| Total formula weight | 25418.06 |
| Authors | Han, Q.,Robinson, R.,Li, J. (deposition date: 2012-05-26, release date: 2012-06-27, Last modification date: 2023-09-13) |
| Primary citation | Han, Q.,Robinson, H.,Ding, H.,Christensen, B.M.,Li, J. Evolution of insect arylalkylamine N-acetyltransferases: structural evidence from the yellow fever mosquito, Aedes aegypti. Proc.Natl.Acad.Sci.USA, 109:11669-11674, 2012 Cited by PubMed Abstract: 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 β3 and β4 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. PubMed: 22753468DOI: 10.1073/pnas.1206828109 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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