Sandbox Reserved 768: Difference between revisions

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== Phenylalanine Hydroxylase Structure ==

Although the full-length structure of mammalian PAH has not yet been clearly known, a large part of it has been identified. <ref name= "flydal"/>. It was solved by means of crystallizing the protein (at pH=7) to perform X-ray ~~chromatography~~ using molecular replacement. The search model used was based on the crystal structure of tyrosine hydroxylase because of the similarity between the two enzymes. <ref name="fusetti"> Fusetti, Fabrizia, Heidi Erlandsen, Torgeir Flatmark, and Raymond Stevens. "Structure of Tetrameric Human Phenylalanine Hydroxylase and Its Implications for Phenylketonuria." The Journal of Biological Chemistry 273.27 (1998): 16962-16967. Web. </ref>. The R-factor recorded was 0.251 and the mean B (or temperature) value was 33.0. <ref name= "pdb"/>.

Although the full-length structure of mammalian PAH has not yet been clearly known, a large part of it has been identified. <ref name= "flydal"/>. It was solved by means of crystallizing the protein (at pH=7) to perform X-ray diffraction using molecular replacement. The search model used was based on the crystal structure of tyrosine hydroxylase because of the similarity between the two enzymes. <ref name="fusetti"> Fusetti, Fabrizia, Heidi Erlandsen, Torgeir Flatmark, and Raymond Stevens. "Structure of Tetrameric Human Phenylalanine Hydroxylase and Its Implications for Phenylketonuria." The Journal of Biological Chemistry 273.27 (1998): 16962-16967. Web. </ref>. The R-factor recorded was 0.251 and the mean B (or temperature) value was 33.0. <ref name= "pdb"/>.

'''Structure Revealed'''

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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"/>.

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 28: / Line 28: @@
 == Phenylalanine Hydroxylase Structure ==
-Although the full-length structure of mammalian PAH has not yet been clearly known, a large part of it has been identified. <ref name= "flydal"/>. It was solved by means of crystallizing the protein (at pH=7) to perform X-ray chromatography using molecular replacement. The search model used was based on the crystal structure of tyrosine hydroxylase because of the similarity between the two enzymes. <ref name="fusetti"> Fusetti, Fabrizia, Heidi Erlandsen, Torgeir Flatmark, and Raymond Stevens. "Structure of Tetrameric Human Phenylalanine Hydroxylase and Its Implications for Phenylketonuria." The Journal of Biological Chemistry 273.27 (1998): 16962-16967. Web. </ref>. The R-factor recorded was 0.251 and the mean B (or temperature) value was 33.0. <ref name= "pdb"/>.
+Although the full-length structure of mammalian PAH has not yet been clearly known, a large part of it has been identified. <ref name= "flydal"/>. It was solved by means of crystallizing the protein (at pH=7) to perform X-ray diffraction using molecular replacement. The search model used was based on the crystal structure of tyrosine hydroxylase because of the similarity between the two enzymes. <ref name="fusetti"> Fusetti, Fabrizia, Heidi Erlandsen, Torgeir Flatmark, and Raymond Stevens. "Structure of Tetrameric Human Phenylalanine Hydroxylase and Its Implications for Phenylketonuria." The Journal of Biological Chemistry 273.27 (1998): 16962-16967. Web. </ref>. The R-factor recorded was 0.251 and the mean B (or temperature) value was 33.0. <ref name= "pdb"/>.
 '''Structure Revealed'''
@@ 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"/>.
+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"/>.