6XRX

Crystal structure of the mosquito protein AZ1 as an MBP fusion

6XRX の概要

• エントリーDOI: 10.2210/pdb6xrx/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose/maltodextrin-binding periplasmic protein, Mosquito protein AZ1, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: mosquito, fatty acids, lipids, anti-viral, lipid binding protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 61850.49

構造登録者

Pedersen, L.C.,Mueller, G.A.,Foo, A.C.Y. (登録日: 2020-07-14, 公開日: 2021-03-24, 最終更新日: 2023-10-18)

主引用文献

Foo, A.C.Y.,Thompson, P.M.,Chen, S.H.,Jadi, R.,Lupo, B.,DeRose, E.F.,Arora, S.,Placentra, V.C.,Premkumar, L.,Perera, L.,Pedersen, L.C.,Martin, N.,Mueller, G.A.
The mosquito protein AEG12 displays both cytolytic and antiviral properties via a common lipid transfer mechanism.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: The mosquito protein AEG12 is up-regulated in response to blood meals and flavivirus infection though its function remained elusive. Here, we determine the three-dimensional structure of AEG12 and describe the binding specificity of acyl-chain ligands within its large central hydrophobic cavity. We show that AEG12 displays hemolytic and cytolytic activity by selectively delivering unsaturated fatty acid cargoes into phosphatidylcholine-rich lipid bilayers. This property of AEG12 also enables it to inhibit replication of enveloped viruses such as Dengue and Zika viruses at low micromolar concentrations. Weaker inhibition was observed against more distantly related coronaviruses and lentivirus, while no inhibition was observed against the nonenveloped virus adeno-associated virus. Together, our results uncover the mechanistic understanding of AEG12 function and provide the necessary implications for its use as a broad-spectrum therapeutic against cellular and viral targets.

PubMed: 33688047
DOI: 10.1073/pnas.2019251118

実験手法

X-RAY DIFFRACTION (1.95 Å)