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-Structure paper
タイトル | CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase. |
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ジャーナル・号・ページ | Nat Commun, Vol. 13, Issue 1, Page 6185, Year 2022 |
掲載日 | 2022年10月19日 |
著者 | Jorge Pedro López-Alonso / Melisa Lázaro / David Gil-Cartón / Philip H Choi / Alexandra Dodu / Liang Tong / Mikel Valle / |
PubMed 要旨 | Pyruvate carboxylase (PC) is a tetrameric enzyme that contains two active sites per subunit that catalyze two consecutive reactions. A mobile domain with an attached prosthetic biotin links both ...Pyruvate carboxylase (PC) is a tetrameric enzyme that contains two active sites per subunit that catalyze two consecutive reactions. A mobile domain with an attached prosthetic biotin links both reactions, an initial biotin carboxylation and the subsequent carboxyl transfer to pyruvate substrate to produce oxaloacetate. Reaction sites are at long distance, and there are several co-factors that play as allosteric regulators. Here, using cryoEM we explore the structure of active PC tetramers focusing on active sites and on the conformational space of the oligomers. The results capture the mobile domain at both active sites and expose catalytic steps of both reactions at high resolution, allowing the identification of substrates and products. The analysis of catalytically active PC tetramers reveals the role of certain motions during enzyme functioning, and the structural changes in the presence of additional cofactors expose the mechanism for allosteric regulation. |
リンク | Nat Commun / PubMed:36261450 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.12 - 3.29 Å |
構造データ | EMDB-15028, PDB-7zyy: EMDB-15029, PDB-7zyz: EMDB-15030, PDB-7zz0: EMDB-15031, PDB-7zz1: EMDB-15032, PDB-7zz2: EMDB-15033, PDB-7zz3: EMDB-15034, PDB-7zz4: EMDB-15035, PDB-7zz5: EMDB-15036, PDB-7zz6: EMDB-15037, PDB-7zz8: |
化合物 | ChemComp-MG: ChemComp-MN: ChemComp-ADP: ChemComp-ACO: ChemComp-PYR: ChemComp-BCT: ChemComp-HOH: ChemComp-OAA: ChemComp-BTN: ChemComp-ATP: ChemComp-2BA: |
由来 |
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キーワード | LIGASE / Tetramer / carboxylase / biotin / inhibitor |