5CF9

Cleavage of nicotinamide adenine dinucleotide by the ribosome inactivating protein of Momordica charantia - enzyme-NADP+ co-crystallisation.

5CF9 の概要

• エントリーDOI: 10.2210/pdb5cf9/pdb
• 関連するPDBエントリー: 4YPT
• 分子名称: Ribosome-inactivating protein momordin I, 2-acetamido-2-deoxy-beta-D-glucopyranose, NICOTINAMIDE, ... (4 entities in total)
• 機能のキーワード: product, complex, glycosidase, nadp, hydrolase
• 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: 27739.62

構造登録者

Vinkovic, M.,Wood, S.P.,Gill, R.,Husain, J.,Wood, G.E.,Dunn, G. (登録日: 2015-07-08, 公開日: 2015-07-22, 最終更新日: 2024-01-10)

主引用文献

Vinkovic, M.,Dunn, G.,Wood, G.E.,Husain, J.,Wood, S.P.,Gill, R.
Cleavage of nicotinamide adenine dinucleotide by the ribosome-inactivating protein from Momordica charantia.
Acta Crystallogr.,Sect.F, 71:1152-1155, 2015

PubMed Abstract: The interaction of momordin, a type 1 ribosome-inactivating protein from Momordica charantia, with NADP(+) and NADPH has been investigated by X-ray diffraction analysis of complexes generated by co-crystallization and crystal soaking. It is known that the proteins of this family readily cleave the adenine-ribose bond of adenosine and related nucleotides in the crystal, leaving the product, adenine, bound to the enzyme active site. Surprisingly, the nicotinamide-ribose bond of oxidized NADP(+) is cleaved, leaving nicotinamide bound in the active site in the same position but in a slightly different orientation to that of the five-membered ring of adenine. No binding or cleavage of NADPH was observed at pH 7.4 in these experiments. These observations are in accord with current views of the enzyme mechanism and may contribute to ongoing searches for effective inhibitors.

PubMed: 26323301
DOI: 10.1107/S2053230X15013540

実験手法

X-RAY DIFFRACTION (1.52 Å)