3EU5

Crystal structure of FTase(ALPHA-subunit; BETA-subunit DELTA C10) in complex with BiotinGPP

3EU5 の概要

• エントリーDOI: 10.2210/pdb3eu5/pdb
• 関連するPDBエントリー: 3EUV
• 分子名称: Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha, Protein farnesyltransferase subunit beta, ZINC ION, ... (5 entities in total)
• 機能のキーワード: protein prenylation, prenylome analysis, prenyltransferase, transferase, metal-binding, phosphoprotein, zinc
• 由来する生物種: Rattus norvegicus (Rat); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92468.41

構造登録者

Guo, Z.,Nguyen, U.T.T.,Delon, C.,Bon, R.S.,Blankenfeldt, W.,Goody, R.S.,Waldmann, H.,Wolters, D.,Alexandrov, K. (登録日: 2008-10-09, 公開日: 2009-07-07, 最終更新日: 2023-11-01)

主引用文献

Nguyen, U.T.T.,Guo, Z.,Delon, C.,Wu, Y.,Deraeve, C.,Franzel, B.,Bon, R.S.,Blankenfeldt, W.,Goody, R.S.,Waldmann, H.,Wolters, D.,Alexandrov, K.
Analysis of the eukaryotic prenylome by isoprenoid affinity tagging
Nat.Chem.Biol., 5:227-235, 2009

PubMed Abstract: Protein prenylation is a widespread phenomenon in eukaryotic cells that affects many important signaling molecules. We describe the structure-guided design of engineered protein prenyltransferases and their universal synthetic substrate, biotin-geranylpyrophosphate. These new tools allowed us to detect femtomolar amounts of prenylatable proteins in cells and organs and to identify their cognate protein prenyltransferases. Using this approach, we analyzed the in vivo effects of protein prenyltransferase inhibitors. Whereas some of the inhibitors displayed the expected activities, others lacked in vivo activity or targeted a broader spectrum of prenyltransferases than previously believed. To quantitate the in vivo effect of the prenylation inhibitors, we profiled biotin-geranyl-tagged RabGTPases across the proteome by mass spectrometry. We also demonstrate that sites of active vesicular transport carry most of the RabGTPases. This approach enables a quantitative proteome-wide analysis of the regulation of protein prenylation and its modulation by therapeutic agents.

PubMed: 19219049
DOI: 10.1038/nchembio.149

実験手法

X-RAY DIFFRACTION (2.8 Å)