4U04

Structure of a eukaryotic fic domain containing protein

4U04 の概要

• エントリーDOI: 10.2210/pdb4u04/pdb
• 分子名称: Adenosine monophosphate-protein transferase FICD, D(-)-TARTARIC ACID, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: adenylation, tpr, fic, transferase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Membrane ; Single-pass membrane protein : Q9BVA6
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79635.09

構造登録者

Cole, A.R.,Bunney, T.D.,Katan, M. (登録日: 2014-07-11, 公開日: 2014-12-10, 最終更新日: 2023-12-20)

主引用文献

Bunney, T.D.,Cole, A.R.,Broncel, M.,Esposito, D.,Tate, E.W.,Katan, M.
Crystal structure of the human, FIC-domain containing protein HYPE and implications for its functions.
Structure, 22:1831-1843, 2014

PubMed Abstract: Protein AMPylation, the transfer of AMP from ATP to protein targets, has been recognized as a new mechanism of host-cell disruption by some bacterial effectors that typically contain a FIC-domain. Eukaryotic genomes also encode one FIC-domain protein,HYPE, which has remained poorly characterized.Here we describe the structure of human HYPE, solved by X-ray crystallography, representing the first structure of a eukaryotic FIC-domain protein. We demonstrate that HYPE forms stable dimers with structurally and functionally integrated FIC-domains and with TPR-motifs exposed for protein-protein interactions. As HYPE also uniquely possesses a transmembrane helix, dimerization is likely to affect its positioning and function in the membrane vicinity. The low rate of auto AMPylation of the wild-type HYPE could be due to autoinhibition, consistent with the mechanism proposed for a number of putative FIC AMPylators. Our findings also provide a basis to further consider possible alternative cofactors of HYPE and distinct modes of target-recognition.

PubMed: 25435325
DOI: 10.1016/j.str.2014.10.007

実験手法

X-RAY DIFFRACTION (2.48 Å)