2013/09/17

転載:アコニターゼと鉄調節タンパク質1

TCA回路についてまとめているときにみつけたアコニターゼの解説がとても興味深かったので,日本蛋白質構造データバンク (PDBj )から関連するテキストの部分を転載します。元記事は http://pdbj.org/mom?id=89 で,こっちにはもっと図があります。

本当に知りたかったのは,アコニターゼがクエン酸を異性化する際に,アセチルCoA由来の炭素とオキサロ酢酸由来の炭素を見分けるのかどうかだったので,このへんは調べて追記したいと思います。


***ここから***

アコニターゼは トリカルボン酸回路(TCA回路、クエン酸回路) に欠かせない酵素で、鉄制御蛋白質1はメッセンジャーRNAと相互作用し細胞内の鉄濃度を制御する蛋白質である。あなたはこのように尋ねるかもしれない。この2つの蛋白質にどのような共通点があるのかと。この2つの蛋白質は別々の研究者によって発見され研究されたもので、それぞれが持つ互いに大きく違った機能を示す名前が付けられている。ところが驚くべきことに、この2つの蛋白質のアミノ酸配列を見ると、同じであることが分かった。同じ蛋白質が非常に異なる2種類の仕事をしているのである。

アコニターゼ...

アコニターゼ酵素はエネルギーを作り出す中心的反応において重要な役割を果たしている。トリカルボン酸回路の途中で、この酵素はクエン酸をイソクエン酸に変換する。アコニターゼの1つの型が、我々の持つミトコンドリアで見られる。ここではクエン酸回路のほとんどが行われる。一方類似の型が細胞質で見られ、ここでは他の合成作業に使われるイソクエン酸が作られる。右図上に示したのが細胞基質型の構造で、PDBエントリー 2b3y のものである。この蛋白質は複数のドメインで構成された1本のペプチド鎖でできている(ドメインは青の濃さを変えて区別し示している)。ドメインはくるみ割りのように閉じて活性部位を取り囲んでいる。その活性部位には鉄硫黄クラスターがあって反応を助けている。

...それとも鉄制御蛋白質1

アコニターゼの細胞基質型は鉄制御蛋白質1としても働く。右図下の構造はPDBエントリー 2ipy のもので、どのようにして完全に別の機能を果たしているかを示している。アコニターゼの中にある鉄硫黄クラスターは不安定で、外れる時に時々交換しなければならない。細胞内の鉄濃度が低くなると、鉄硫黄クラスターを再生成するだけの鉄が不足し、アコニターゼは第2の機能を行うよう変化する。蛋白質は開き、特有のメッセンジャーRNA分子の中にあるヘアピンループをつかむ。これには フェリチン (ferritin)のメッセンジャーRNAの開始部位にあるヘアピンと、 トランスフェリン受容体 (transferrin receptor)のメッセンジャーRNAの末端にある似た5つのヘアピンが含まれる。鉄制御蛋白質1が結合すると、フェリチンの形成が阻害されて鉄の蓄積が減少し、トランスフェリン受容体の構築が促進される。その結果、細胞は血液からより多くのトランスフェリンを取り上げ、同時により多くの鉄を取り込むことになる。

mom089_04.jpg

アコニターゼは、生化学の教科書で例としてよく使われる古典的で立体特異的な反応を行う。クエン酸からヒドロキシル基(-OH)と特有の水素原子を取り出し、立体化学的に正確な方法で入れ替えてイソクエン酸を作る。この反応は2つの結晶構造によって明らかにされたが、これを見るに当たって少し想像力を働かせる必要がある。なぜなら結晶構造には水素原子の位置情報は含まれていないからである。上図左に示したPDBエントリー 1c96 の構造では活性部位にクエン酸が結合している。この酵素は通常型の場合、酸素原子(ピンク色)が鉄硫黄クラスターによって、水素原子が上にあるセリンによって取り出される(両反応を緑の矢印で示した)。但し、この構造はセリンがアラニンに置き換わった変異体であるため、セリンでは存在するはずの酸素原子がみられない。2つ目の反応では、上図右に示したPDBエントリー 7acn のように、分子が反転して上下が逆になり(A-B-C と標識された位置が変わっているのに注意)、水素とヒドロキシル基が異なる場所に付け戻されてイソクエン酸ができる。

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