3SJ6

Crystal Structure of the complex of type I ribosome inactivating protein from momordica balsamina with 5-(hydroxymethyl)oxalane-2,3,4-triol at 1.6 A resolution

3SJ6 の概要

• エントリーDOI: 10.2210/pdb3sj6/pdb
• 関連するPDBエントリー: 1AHA
• 分子名称: Ribosome inactivating protein, 2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-ribopyranose, ... (5 entities in total)
• 機能のキーワード: rip, rna n-glycosidase, plant protein, ribose, inactivation, hydrolase
• 由来する生物種: Momordica balsamina (Bitter gourd)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27649.28

構造登録者

Pandey, N.,Kushwaha, G.S.,Sinha, M.,Kaur, P.,Sharma, S.,Singh, T.P. (登録日: 2011-06-21, 公開日: 2011-08-03, 最終更新日: 2024-10-30)

主引用文献

Kushwaha, G.S.,Pandey, N.,Sinha, M.,Singh, S.B.,Kaur, P.,Sharma, S.,Singh, T.P.
Crystal structures of a type-1 ribosome inactivating protein from Momordica balsamina in the bound and unbound states.
Biochim.Biophys.Acta, 1824:679-691, 2012

PubMed Abstract: The ribosome inactivating proteins (RIPs) of type 1 are plant toxins that eliminate adenine base selectively from the single stranded loop of rRNA. We report six crystal structures, type 1 RIP from Momordica balsamina (A), three in complexed states with ribose (B), guanine (C) and adenine (D) and two structures of MbRIP-1 when crystallized with adenosine triphosphate (ATP) (E) and 2'-deoxyadenosine triphosphate (2'-dATP) (F). These were determined at 1.67Å, 1.60Å, 2.20Å, 1.70Å, 2.07Å and 1.90Å resolutions respectively. The structures contained, (A) unbound protein molecule, (B) one protein molecule and one ribose sugar, (C) one protein molecule and one guanine base, (D) one protein molecule and one adenine base, (E) one protein molecule and one ATP-product adenine molecule and (F) one protein molecule and one 2'-dATP-product adenine molecule. Three distinct conformations of the side chain of Tyr70 were observed with (i) χ(1)=-66°and χ(2)=165° in structures (A) and (B); (ii) χ(1)=-95° and χ(2)=70° in structures (C), (D) and (E); and (iii) χ(1)=-163° and χ(2)=87° in structure (F). The conformation of Tyr70 in (F) corresponds to the structure of a conformational intermediate. This is the first structure which demonstrates that the slow conversion of DNA substrates by RIPs can be trapped during crystallization.

PubMed: 22361570
DOI: 10.1016/j.bbapap.2012.02.005

実験手法

X-RAY DIFFRACTION (1.6 Å)