Sandbox Reserved 1734: Difference between revisions
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Secondary Structure: | Secondary Structure: | ||
Phenylalanine hydroxylase (PAH) contains right-handed alpha helices and antiparallel beta-strands in its secondary structure (5 & 6). There are some amino acids that don't have any secondary structure, and these are found in the loop containing regions. The loop containing regions are residues | Phenylalanine hydroxylase (PAH) contains right-handed alpha helices and antiparallel beta-strands in its secondary structure (5 & 6). There are some amino acids that don't have any secondary structure, and these are found in the loop containing regions. The loop containing regions are residues Leucine 42-Valine 45, Aspartic acid 59-Histidine 69, Serine 70-Aspartic acid 75, and Histidine 82-Valine 90 (5). | ||
Tertiary Structure: | Tertiary Structure: | ||
The tertiary structure of each monomer of PAH is organized from 2 alpha helices and 4 beta-strands into an alpha-beta sandwich motif (BaBBaB fold). The structural motif of an alpha-beta sandwich motif has the 4 antiparallel beta-strands flanked on one side by the 2 alpha-helices (3 & 5). The tertiary structure of a phenylalanine hydroxylase protein is built from an N-terminal regulatory domain (residues 1-117), a catalytic domain (residues 118-410), and a tetramerization domain (residues 411-452) (1 & 5). The catalytic domain includes the binding sites for iron, substrate and cofactor. The binding sites are at residues 285, 290, and 330. The ACT domain is in the N-terminal regulatory domain where proposed enzyme binding to an allosteric site (residues 3-11) (1). | The tertiary structure of each monomer of PAH is organized from 2 alpha helices and 4 beta-strands into an alpha-beta sandwich motif (BaBBaB fold). The structural motif of an alpha-beta sandwich motif has the 4 antiparallel beta-strands flanked on one side by the 2 alpha-helices (3 & 5). The tertiary structure of a phenylalanine hydroxylase protein is built from an N-terminal regulatory domain (residues 1-117), a catalytic domain (residues 118-410), and a tetramerization domain (residues 411-452) (1 & 5). The catalytic domain includes the binding sites for iron, substrate and cofactor. The binding sites are at residues 285, 290, and 330. The archetypical (ACT) domain is in the N-terminal regulatory domain where proposed enzyme binding to an allosteric site (residues 3-11) (1). | ||
Quaternary Structure: | Quaternary Structure: | ||
