Sandbox Reserved 1566

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This Sandbox is Reserved from Aug 26 through Dec 12, 2019 for use in the course CHEM 351 Biochemistry taught by Bonnie_Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1556 through Sandbox Reserved 1575.
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Stucture of 6MLT

Secondary structure is important in Bap1. 6MLT is composed of two major domains, the beta-prism domain and the beta-propeller domain. Yellow represents the beta-helix, with pink showing the alpha-helix, white showing coils and loops, and turns in blue.

One of the major functions of Bap1 is it's sugar binding properties. This image shows the binding pocket on the beta-prism, which is where carbohydrates bind. The molecule is shown in spacefill and is colored based on hydrophobicity. Hydrophilic residues are shown in blue, with hydrophobic residues in red, and non charged residues in white. Lys, which makes up a large part of the binding pocket is represented in pink. The positively charged side chain on Lys makes it great for negatively charged sugars to bind to.


Asp 348, which is found on the beta-prism of Bap1, plays a crucial role in binding to citrate and carbohydrates. Mutation of aspartic acid to alanine results in a loss of function for Bap1. Since Ala has a much smaller side chain than Asp, it becomes too many Å away to interact.


Caption for this structure

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References

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