Sandbox Reserved 1072: Difference between revisions

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===Monomer Structure===

The two [http://en.wikipedia.org/wiki/Protein_domain domains] of each monomer are primarily [http://en.wikipedia.org/wiki/Alpha_helix alpha helical] and have similar foldings. The similar foldings suggests that the monomer results from a [http://en.wikipedia.org/wiki/Gene_duplication gene duplication] event; however, the C-terminal domain does not contain the [http://en.wikipedia.org/wiki/Heme_B heme ''b''] prosthetic group, while the <scene name='69/694238/N_terminus/1'>N terminal</scene> does. The [~~http://en.wikipedia.org/wiki/Active_site~~ active site] is therefore located within the N-terminal domain. The two monomers interact through an interlocking hook formed by the N-terminal domains that stabilizes the formation of the dimer (1).

The two [http://en.wikipedia.org/wiki/Protein_domain domains] of each monomer are primarily [http://en.wikipedia.org/wiki/Alpha_helix alpha helical] and have similar foldings. The similar foldings suggests that the monomer results from a [http://en.wikipedia.org/wiki/Gene_duplication gene duplication] event; however, the C-terminal domain does not contain the [http://en.wikipedia.org/wiki/Heme_B heme ''b''] prosthetic group, while the <scene name='69/694238/N_terminus/1'>N terminal</scene> does. The [[active site]] is therefore located within the N-terminal domain. The two monomers interact through an interlocking hook formed by the N-terminal domains that stabilizes the formation of the dimer (1).

The N-terminal <scene name='69/694238/N_terminus/2'>hook</scene> is formed through hydrophobic interactions between residues Tyr-28 and Tyr-197 and residues Trp-38 and Trp-204. This interlocking loop region is also found in similar conformations of other catalase peroxidase structures such as: [http://www.proteopedia.org/wiki/index.php/1itk ''hm''CP] and ''bp''CP.

Sandbox Reserved 1072: Difference between revisions

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@@ Line 10: / Line 10: @@
 ===Monomer Structure===
-The two [http://en.wikipedia.org/wiki/Protein_domain domains] of each monomer are primarily [http://en.wikipedia.org/wiki/Alpha_helix alpha helical] and have similar foldings. The similar foldings suggests that the monomer results from a [http://en.wikipedia.org/wiki/Gene_duplication gene duplication] event; however, the C-terminal domain does not contain the [http://en.wikipedia.org/wiki/Heme_B heme ''b''] prosthetic group, while the <scene name='69/694238/N_terminus/1'>N terminal</scene> does. The [http://en.wikipedia.org/wiki/Active_site active site] is therefore located within the N-terminal domain. The two monomers interact through an interlocking hook formed by the N-terminal domains that stabilizes the formation of the dimer (1).
+The two [http://en.wikipedia.org/wiki/Protein_domain domains] of each monomer are primarily [http://en.wikipedia.org/wiki/Alpha_helix alpha helical] and have similar foldings. The similar foldings suggests that the monomer results from a [http://en.wikipedia.org/wiki/Gene_duplication gene duplication] event; however, the C-terminal domain does not contain the [http://en.wikipedia.org/wiki/Heme_B heme ''b''] prosthetic group, while the <scene name='69/694238/N_terminus/1'>N terminal</scene> does. The [[active site]] is therefore located within the N-terminal domain. The two monomers interact through an interlocking hook formed by the N-terminal domains that stabilizes the formation of the dimer (1).
 The N-terminal <scene name='69/694238/N_terminus/2'>hook</scene> is formed through hydrophobic interactions between residues Tyr-28 and Tyr-197 and residues Trp-38 and Trp-204. This interlocking loop region is also found in similar conformations of other catalase peroxidase structures such as: [http://www.proteopedia.org/wiki/index.php/1itk ''hm''CP] and ''bp''CP.