Sandbox Reserved 765

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==Structural Content==
==Structural Content==
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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. The monomer structure is composed of 35% <scene name='56/564041/Helices/1'>helices</scene> (16 helices) and 18% beta sheet (20 strands).
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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. The monomer structure is composed of 35% helices (16 helices) and 18% beta sheet (20 strands).
[[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.]]

Revision as of 02:43, 4 December 2013

This Sandbox is Reserved from Sep 25, 2013, through Mar 31, 2014 for use in the course "BCH455/555 Proteins and Molecular Mechanisms" taught by Michael B. Goshe at the North Carolina State University. This reservation includes Sandbox Reserved 299, Sandbox Reserved 300 and Sandbox Reserved 760 through Sandbox Reserved 779.
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Chorismate Synthase


Structure of HMG-CoA reductase (PDB entry 1dq8)

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