Sandbox Reserved 768: Difference between revisions
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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"/>. | ||
The residues surrounding the iron atom in the active site are: PHE 254, ARG 270, HIS 285, GLU 286, TRP 326, and GLU 330. <ref name= "flydal"/>. The illustration below highlights these residues and their relative positions to the iron atom, BH4 cofactor, and the L-Phenyalanine substrate | The residues surrounding the iron atom in the active site are: PHE 254, ARG 270, HIS 285, GLU 286, TRP 326, and GLU 330. <ref name= "flydal"/>. The illustration below highlights these residues and their relative positions to the iron atom, BH4 cofactor, and the L-Phenyalanine substrate. | ||
[[Image:Active residues.jpg]] | |||
