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 tetramer 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/2'>helices</scene> (17 helices) and 18% <scene name='56/564041/Beta_sheets/1'>beta sheets</scene> (21 strands).

All of the beta sheets within each monomer run anti-parallel with one another. Helices are divided into two categories: alpha helices and 3/10 helices. In the structure there are eleven alpha helices and

there are six 3/10 helices. The image to the right displays the sequence of chorismate synthase. We can examine the two structures, <scene name='56/564041/Unbound_chorismate_synthase/1'>unbound</scene> chorismate synthase and with mycobacterium tuberculosis <scene name='56/564041/Bound_chorismate_synthase/1'>bound</scene> and FMN bound.

there are six 3/10 helices. The image to the right displays the sequence of chorismate synthase. We can examine the two structures, <scene name='56/564041/Unbound_chorismate_synthase/1'>unbound</scene> chorismate synthase and with mycobacterium tuberculosis <scene name='56/564041/Bound_chorismate_synthase/1'>bound</scene> and FMN bound. The <scene name='56/564041/N-c_terminal/1'>N and C terminus</scene> are both present within each monomer and goes from blue to red.

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 tetramer 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/2'>helices</scene> (17 helices) and 18% <scene name='56/564041/Beta_sheets/1'>beta sheets</scene> (21 strands).
 All of the beta sheets within each monomer run anti-parallel with one another. Helices are divided into two categories: alpha helices and 3/10 helices. In the structure there are eleven alpha helices and
-there are six 3/10 helices. The image to the right displays the sequence of chorismate synthase. We can examine the two structures, <scene name='56/564041/Unbound_chorismate_synthase/1'>unbound</scene> chorismate synthase and with mycobacterium tuberculosis <scene name='56/564041/Bound_chorismate_synthase/1'>bound</scene> and FMN bound.
+there are six 3/10 helices. The image to the right displays the sequence of chorismate synthase. We can examine the two structures, <scene name='56/564041/Unbound_chorismate_synthase/1'>unbound</scene> chorismate synthase and with mycobacterium tuberculosis <scene name='56/564041/Bound_chorismate_synthase/1'>bound</scene> and FMN bound. The <scene name='56/564041/N-c_terminal/1'>N and C terminus</scene> are both present within each monomer and goes from blue to red.