7zz5

Cryo-EM structure of "BC open" conformation of Lactococcus lactis pyruvate carboxylase with acetyl-CoA

spinqualitylabelsall models 7zz5, resolution 2.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7zz5 is a 1 chain structure with sequence from Lactococcus lactis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.43Å Ligands: ACO, BCT, KCX Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase.,Lopez-Alonso JP, Lazaro M, Gil-Carton D, Choi PH, Dodu A, Tong L, Valle M Nat Commun. 2022 Oct 19;13(1):6185. doi: 10.1038/s41467-022-33987-2. PMID:36261450 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pyruvate carboxylase 3D structures

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