Sandbox Reserved 768: Difference between revisions

Line 10:

[[Image:PAH tetramer complex.jpg]]

Each monomeric subunit is composed of three sites: the N-terminal, the catalytic site, and the C-terminal. <ref name= "flydal"/>.

Each monomeric subunit is composed of three sites: the N-terminal, the catalytic site, and the C-terminal. <ref name= " flydal"/>.

PAH enzyme has been studied extensively because of its correlation with the genetic defective condition phenylketonuria (PKU). Errors in the function or stability of PAH lead to its malfunction which causes a buildup of phenylalanine resulting in numerous health detriments.

Line 44:

The C-terminal oligomerization or tetramerization domain begins with an antiparallel-sheet

(residues 411–414, 421–424)

and is formed by a C-terminal “arm” consisting of two β-strands, forming a β-ribbon, and a 40 Å long α-helix. This C-terminal arm extends over an adjacent monomer, thus bringing the four helices (one from each monomer) into a closely packed anti-parallel coiled-coil motif in the center of the structure (as can be seen in the tetramer structure above). <ref name= "fusetti"/>. The assembly of the enzyme occurs through a swapping mechanism in which the secondary structural elements mutually switch their position to promote oligomerization. <ref name="fusetti"/>.

and is formed by a C-terminal “arm” consisting of two β-strands, forming a β-ribbon, and a 40 Å long α-helix. This C-terminal arm extends over an adjacent monomer, thus bringing the four helices (one from each monomer) into a closely packed anti-parallel coiled-coil motif in the center of the structure (as can be seen in the tetramer structure above). <ref name= "fusetti"/>. The assembly of the enzyme occurs through a swapping mechanism in which the secondary structural elements mutually switch their position to promote oligomerization. <ref name= "fusetti"/>.

Sandbox Reserved 768: Difference between revisions

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@@ Line 10: / Line 10: @@
 [[Image:PAH tetramer complex.jpg]]
-Each monomeric subunit is composed of three sites: the N-terminal, the catalytic site, and the C-terminal. <ref name= "flydal"/>.
+Each monomeric subunit is composed of three sites: the N-terminal, the catalytic site, and the C-terminal. <ref name= " flydal"/>.
 PAH enzyme has been studied extensively because of its correlation with the genetic defective condition phenylketonuria (PKU). Errors in the function or stability of PAH lead to its malfunction which causes a buildup of phenylalanine resulting in numerous health detriments.
@@ Line 44: / Line 44: @@
 The C-terminal oligomerization or tetramerization domain begins with an antiparallel-sheet
 (residues 411–414, 421–424)
-and is formed by a C-terminal “arm” consisting of two β-strands, forming a β-ribbon, and a 40 Å long α-helix. This C-terminal arm extends over an adjacent monomer, thus bringing the four helices (one from each monomer) into a closely packed anti-parallel coiled-coil motif in the center of the structure (as can be seen in the tetramer structure above). <ref name= "fusetti"/>. The assembly of the enzyme occurs through a swapping mechanism in which the secondary structural elements mutually switch their position to promote oligomerization. <ref name="fusetti"/>.
+and is formed by a C-terminal “arm” consisting of two β-strands, forming a β-ribbon, and a 40 Å long α-helix. This C-terminal arm extends over an adjacent monomer, thus bringing the four helices (one from each monomer) into a closely packed anti-parallel coiled-coil motif in the center of the structure (as can be seen in the tetramer structure above). <ref name= "fusetti"/>. The assembly of the enzyme occurs through a swapping mechanism in which the secondary structural elements mutually switch their position to promote oligomerization. <ref name= "fusetti"/>.