6LOW

crystal structure of alpha-momorcharin in complex with GMP

6LOW の概要

• エントリーDOI: 10.2210/pdb6low/pdb
• 分子名称: Ribosome-inactivating protein momordin I, 2-acetamido-2-deoxy-beta-D-glucopyranose, GUANOSINE-5'-MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: alpha-momorcharin, ribosome-inactivating protein, rrna n-glycosidase, gmp, plant protein
• 由来する生物種: Momordica charantia (Bitter gourd)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32147.39

構造登録者

Fan, X.,Jin, T. (登録日: 2020-01-07, 公開日: 2020-11-18, 最終更新日: 2024-10-23)

主引用文献

Fan, X.,Wang, Y.,Guo, F.,Zhang, Y.,Jin, T.
Atomic-resolution structures of type I ribosome inactivating protein alpha-momorcharin with different substrate analogs.
Int.J.Biol.Macromol., 164:265-276, 2020

PubMed Abstract: Alpha-momorcharin (Alpha-MMC) from the seed of bitter melon is a type I ribosome inactivating protein (RIP) that removes a specific adenine from 28S rRNA and inhibits protein biosynthesis. Here, we report seven crystal complex structures of alpha-MMC with different substrate analogs (adenine, AMP, cAMP, dAMP, ADP, GMP, and xanthosine) at 1.08 Å to 1.52 Å resolution. These structures reveal that not only adenine, but also guanine and their analogs can effectively bind to alpha-MMC. The side chain of Tyr93 adopts two conformations, serving as a switch to open and close the substrate binding pocket of alpha-MMC. Although adenine, AMP, GMP, and guanine are located in a similar active site in different RIPs, residues involved in the interaction between RIPs and substrate analogs are slightly different. Complex structures of alpha-MMC with different substrate analogs solved in this study provide useful information on its enzymatic mechanisms and may enable the development of new inhibitors to treat the poisoning of alpha-MMC.

PubMed: 32653369
DOI: 10.1016/j.ijbiomac.2020.07.063

実験手法

X-RAY DIFFRACTION (1.39 Å)