非メバロナート経路の末端酵素である (E) - 4 - ヒドロキシ - 3 - メチル - バット - 2 - エニルジホスファート還元酵素の構造

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Ingo Rekittke¹, Jochen Wiesner, Rene Röhrich

¹Institut für Klinische Immunologie and Transfusionsmedizin, Justus-Liebig-Universität Giessen, Langhansstrasse 7, 35385 Giessen, Germany.

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|November 28, 2008

まとめ

研究者らは,2-C-メチル-D-エリトリトール-4-リン酸塩 (MEP) 経路に不可欠な酵素である Aquifex aeolicus LytB の構造を決定した. この構造的な洞察は,細菌や寄生虫におけるイソプレノイド生物合成の理解を助けます.

科学分野:

バイオケミストリーバイオケミストリー
構造生物学構造生物学とは
分子進化は分子進化である

背景:

イソプレノイド生物合成には,2つの主要な代謝経路,メバロナートと2C-メチル-D-エリトリトール-4-リン酸 (MEP) が存在する.
MEP経路は,病原性細菌,Plasmodium falciparumのような寄生性原生体,植物において不可欠であるが,動物では存在しない.
LytB (HMBPP還元酵素) は,MEP経路の最終段階を触媒化し,HMBPPをIPPとDMAPPに変換する.

研究の目的:

Aquifex aeolicus LytB.の分子構造を解明するために.
MEP経路の末端酵素の触媒機構に関する構造的な洞察を提供するために.

主な方法:

X線結晶学を用いて,Aquifex aeolicus LytB.の構造を決定した.
高解像度 (1.65 Å) の構造分析が行われました.

主要な成果:

LytBタンパク質はクローバーリーフ/トリフォイル構造を示し,各モノメアは3つのアルファ/ベータドメインを含んでいます.
中央の[Fe3S4]クラスタはCys13,Cys96,Cys193.3によって結合されている.
保存された残留物His42,His124,およびGlu126は活性部位に位置し,基質結合および触媒に関与することが提案されています.

結論:

決定された構造は,主要な触媒残基を明らかにし,基板結合と製品形成のモデルを提供します.
LytBの構造を理解することは,病原体におけるMEP経路をターゲットにするために極めて重要です.

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