Sandbox Reserved 765: Difference between revisions
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==Structural Content== | ==Structural Content== | ||
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. The monomer structure is composed of 35% <scene name='56/564041/Helices/1'>helices</scene>. | 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. The monomer structure is composed of 35% <scene name='56/564041/Helices/1'>helices</scene> (16 helices) and 18% (20 strands) beta sheet. | ||
[[Image:Chorismate synthase sequence.png|thumb|right|240px|Figure 2. This image is representative of the sequence of chorismate synthase.]] | [[Image:Chorismate synthase sequence.png|thumb|right|240px|Figure 2. This image is representative of the sequence of chorismate synthase.]] | ||
