Sandbox Reserved 765: Difference between revisions
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Chorismate synthase is a homo 4-mer structure, which is composed of four identical monomer subunits. The crystal structure of chorismate synthase was solved at 2.0 Å using the multiwavelength anomalous dispersion (MAD) method. Each monomer within the structure has a β-α-β fold motif. One of the four monomers differs in structure slight close to the active site. This difference makes the active site a lot more accessible, making this monomer an “open” conformation. | Chorismate synthase is a homo 4-mer structure, which is composed of four identical monomer subunits. The crystal structure of chorismate synthase was solved at 2.0 Å using the multiwavelength anomalous dispersion (MAD) method. Each monomer within the structure has a β-α-β fold motif. One of the four monomers differs in structure slight close to the active site. This difference makes the active site a lot more accessible, making this monomer an “open” conformation. | ||
[[Image:Chorismate synthase sequence.png | | [[Image:Chorismate synthase sequence.png | 240px]] | ||
The image to the left displays the sequence of chorismate synthase. | |||
==Mechanism== | ==Mechanism== | ||
