Sandbox324: Difference between revisions
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One of the distinctive structural characteristics of this protein is the alpha/beta-hydrolase (ABH) fold. Evidence for this fold consists of its structure (an open β-sheet surrounded by α-helices) and the presence of what is known as the "catalytic triad" (consisting of a nucleophile, an acid, and histidine)<ref>Holmquist, M. Alpha Beta-Hydrolase Fold Enzymes Structures, Functions and Mechanisms. Current Protein and Peptide Science 2000, 1 (2), 209–235. https://doi.org/10.2174/1389203003381405.</ref>. The presence of the active site residues His A 222, Asp A 192, and Ser A 93, as determined by SPRITE, Chimera, etc., confirms the presence of this catalytic triad. | One of the distinctive structural characteristics of this protein is the alpha/beta-hydrolase (ABH) fold. Evidence for this fold consists of its structure (an open β-sheet surrounded by α-helices) and the presence of what is known as the "catalytic triad" (consisting of a nucleophile, an acid, and histidine)<ref>Holmquist, M. Alpha Beta-Hydrolase Fold Enzymes Structures, Functions and Mechanisms. Current Protein and Peptide Science 2000, 1 (2), 209–235. https://doi.org/10.2174/1389203003381405.</ref>. The presence of the active site residues His A 222, Asp A 192, and Ser A 93, as determined by SPRITE, Chimera, etc., confirms the presence of this catalytic triad. | ||
[ | [[Image:Activesite.jpeg]] | ||
'''Figure 6''' Catalytic triad of protein 4DIU | |||
Another distinctive feature of this protein that demonstrates its identity as an esterase is a coil that correlates to the bioinformatic predictions of Chimera, BLAST, Dali, and Sprite. [Aspen, can you add an image of the coil?] | Another distinctive feature of this protein that demonstrates its identity as an esterase is a coil that correlates to the bioinformatic predictions of Chimera, BLAST, Dali, and Sprite. [Aspen, can you add an image of the coil?] | ||
Swiss Dock and Chimera predicted that this protein would have binding sites with an affinity to substrates such as acetate, butyrate, phosphate, proline, decanoate, dodecanoate, etc. Wet lab experiments still must be conducted in order to confirm these predictions. | Swiss Dock and Chimera predicted that this protein would have binding sites with an affinity to substrates such as acetate, butyrate, phosphate, proline, decanoate, dodecanoate, etc. Wet lab experiments still must be conducted in order to confirm these predictions. | ||
