8apq | pdb_00008apq

CaMct - Mesaconyl-CoA C1:C4 CoA Transferase of Chloroflexus aurantiacus

spinqualitylabelsall models 8apq, resolution 2.49Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8apq is a 6 chain structure with sequence from Chloroflexus aurantiacus J-10-fl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.49Å Ligands: COA, MEZ, OA9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MCT_CHLAA Involved in the glyoxylate assimilation cycle used to regenerate acetyl-CoA and produce pyruvate as universal precursor for biosynthesis. This reaction involves an intramolecular CoA transferase that catalyzes the reversible transfer of the CoA moiety from the C1-carboxyl group of mesaconyl-CoA to the C4-carboxyl group. It does not require free mesaconate as CoA acceptor. Publication Abstract from PubMed Mesaconyl-CoA transferase (Mct) is one of the key enzymes of the 3-hydroxypropionate (3HP) bi-cycle for autotrophic CO(2) fixation. Mct is a family III/Frc family CoA transferase that catalyzes an unprecedented intra-molecular CoA transfer from the C1-carboxyl group to the C4-carboxyl group of mesaconate at catalytic efficiencies >10(6) M(-1) s(-1). Here, we show that the reaction of Mct proceeds without any significant release of free CoA or the transfer to external acceptor acids. Mct catalyzes intra-molecular CoA transfers at catalytic efficiencies that are at least more than 6 orders of magnitude higher compared to inter-molecular CoA transfers, demonstrating that the enzyme exhibits exquisite control over its reaction. To understand the molecular basis of the intra-molecular CoA transfer in Mct, we solved crystal structures of the enzyme from Chloroflexus aurantiacus in its apo form, as well as in complex with mesaconyl-CoA and several covalently enzyme-bound intermediates of CoA and mesaconate at the catalytically active residue Asp165. Based on these structures, we propose a reaction mechanism for Mct that is similar to inter-molecular family III/Frc family CoA transferases. However, in contrast to the latter that undergo opening and closing cycles during the reaction to exchange substrates, the central cavity of Mct remains sealed ("corked-up") by the CoA moiety, strongly favoring the intra-molecular CoA transfer between the C1 and the C4 position of mesaconate. Structural Basis for a Cork-Up Mechanism of the Intra-Molecular Mesaconyl-CoA Transferase.,Pfister P, Zarzycki J, Erb TJ Biochemistry. 2022 Dec 19. doi: 10.1021/acs.biochem.2c00532. PMID:36535006 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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