転写調節器RsrRの結晶構造は,Cys,Glu,およびその残留物によって調整された [2Fe-2S] クラスタを明らかにする
Anne Volbeda1, Ma Teresa Pellicer Martinez2, Jason C Crack2
1Université Grenoble Alpes, CEA, CNRS , IBS , Metalloproteins Unit, F-38044 Grenoble , France.
Journal of the American Chemical Society
|January 19, 2019
まとめ
転写調節器RsrRは,DNA結合制御のためにユニークな [2Fe-2S]クラスタを使用します. この鉄と硫黄の群れは
科学分野:
- 生物化学
- 構造生物学
- 分子生物学
背景:
- Rrf2ファミリーの転写レギュレータ RsrRは遺伝子発現を制御する.
- RsrRの活動は [2Fe-2S] クラスタによって調節され,DNAの結合をリドックス状態の変化でオン/オフにします.
- RsrRの構造を理解することは,その規制メカニズムの解明の鍵です.
研究 の 目的:
- RsrRジメルの高解像度の結晶構造を決定する.
- RsrR内の [2Fe-2S] クラスタの調整を調査する.
- RsrRのDNA結合活動に関連する構造的変化を特定する.
主な方法:
- RsrRジメルの高解像度構造を得るためのX線結晶学.
- [2Fe-2S]クラスタの調整環境を決定するための構造分析.
- 構造の変化を特定するための比較分析
主要な成果:
- Cys,His,およびGlu残基による [2Fe-2S] クラスタの非対称な調整がモノメア-モノメアインターフェイスで明らかになった.
- タンパク質に結合した [Fe-S] クラスタのための新しいリガンド組合せ (3つの異なるアミノ酸サイドチェーン) を特定した.
- DNA結合ヘリックス・ターン・ヘリックス領域に影響を及ぼした.
結論:
- RsrRは,グルタミン酸を含むユニークな [2Fe-2S]クラスター調整を示しており,これは [Fe-S]クラスターにとって初めてのことです.
- 特にTrp9周辺の構造的可塑性は,RsrRの酸化還元依存性DNA結合の基礎となっている.
- これらの発見は,メタルレギュレータのメカニズムと潜在的な薬物標的の洞察を提供します.
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