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- W2005082011 abstract "The crystal structure of muconolactone isomerase from Pseudomonas putida, a unique molecule with ten 96 amino acid subunits and 5-fold, and 2-fold symmetries, has been solved at 3.3 Å resolution. The non-crystallographic symmetries were used to refine the initial single isomorphous replacement phases and produce an interpretable 10-fold averaged map. The backbone trace is complete and confirmed by the amino acid sequence fit. Each subunit is composed of a body with two α-helices and an antiparallel twisted β-sheet of four strands, and an extended arm. The helices and the sheet fold to form a two-layered structure with an enclosed hydrophobic core and a partially formed putative active site pocket. The C-terminal arm of another subunit related by a local dyad symmetry extends over the core to complete this pocket. The decameric protein is almost spherical, with the helices forming the external coat. There is a large hydrophilic cavity in the center with open ends along the 5-fold axis. Molecular interactions between subunits are extensive. Each subunit contacts four neighbors and loses nearly 40% of its solvent contact area on oligomerization." @default.
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- W2005082011 date "1989-02-01" @default.
- W2005082011 modified "2023-10-14" @default.
- W2005082011 title "Crystal structure of muconolactone isomerase at 3.3 Å resolution" @default.
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- W2005082011 doi "https://doi.org/10.1016/0022-2836(89)90226-x" @default.
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