MF7000209 Chorismate mutase (Corynebacterium glutamicum) 5hub X-ray 1.06 Homodimer Corynebacterium glutamicum 29178787 Burschowsky D, Thorbjørnsrud HV, Heim JB, Fahrig-Kamarauskaitė JR, Würth-Roderer K, Kast P, Krengel U Biochemistry 2018 5 57 557-573 Corynebacterium glutamicum is widely used for the industrial production of amino acids, nucleotides, and vitamins. The shikimate pathway enzymes DAHP synthase (CgDS, Cg2391) and chorismate mutase (CgCM, Cgl0853) play a key role in the biosynthesis of aromatic compounds. Here we show that CgCM requires the formation of a complex with CgDS to achieve full activity, and that both CgCM and CgDS are feedback regulated by aromatic amino acids binding to CgDS. Kinetic analysis showed that Phe and Tyr inhibit CgCM activity by inter-enzyme allostery, whereas binding of Trp to CgDS strongly activates CgCM. Mechanistic insights were gained from crystal structures of the CgCM homodimer, tetrameric CgDS, and the heterooctameric CgCM-CgDS complex, refined to 1.1, 2.5, and 2.2 Å resolution, respectively. Structural details from the allosteric binding sites reveal that DAHP synthase is recruited as the dominant regulatory platform to control the shikimate pathway, similar to the corresponding enzyme complex from Mycobacterium tuberculosis. GO:0004106 chorismate mutase activity GO:0046417 chorismate metabolic process GO:0009697 salicylic acid biosynthetic process 2 1 Homooligomeric enzymes Homodimeric enzymes All chains according to the most probable oligomerization state stored in PDBe were considered. A Chorismate mutase Corynebacterium glutamicum Q8NS29 21 99 76% MCMTNAGDNFEIRMPSGTDDPLSDAEIQKYREEINRLDREILDAVKRRTKISQTIGKTRMSSGGTRLVHTREVAIINQFREEIGEEGPALAGILLRMGRGKLG 103 secondary structure helix 10 43 secondary structure helix 48 71 secondary structure helix 73 85 pfam PF01817 Chorismate mutase type II 30 85 A-2 Chorismate mutase Corynebacterium glutamicum Q8NS29 21 99 76% MCMTNAGDNFEIRMPSGTDDPLSDAEIQKYREEINRLDREILDAVKRRTKISQTIGKTRMSSGGTRLVHTREVAIINQFREEIGEEGPALAGILLRMGRGKLG 103 pfam PF01817 Chorismate mutase type II 30 85 Indirect evidence The full structure participates in mutual synergistic folding. Chorismate mutase type II The enzyme is an intertwined dimer of three helices with connecting loops. The N-terminal helices of the two monomers twine together to form an anti-parallel coiled-coil with a hydrophobic interaction surface. The loop between the first and second helices is disordered (PMID:16914555). A N/A A-2 N/A MF7000162 MF7000212 MF7000163 MF7000211 MF7000164 MF7000165 MF7000209 MF7000210