Sandbox Reserved 1072: Difference between revisions

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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 <ref name="one">PMID: 1523184</ref>.  
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/5'>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 <ref name="one">PMID: 1523184</ref>.  


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.
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.
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<scene name='69/694238/Active_site/3'>Arg 104, Trp 107, His 108, His 270, Asp 381</scene> <ref name="one"/>.  
<scene name='69/694238/Active_site/3'>Arg 104, Trp 107, His 108, His 270, Asp 381</scene> <ref name="one"/>.  


<scene name='69/694238/N_terminus/5'>N terminus</scene>


<scene name='69/694238/N_terminus/6'>N terminus stabilization with residues</scene>
<scene name='69/694238/N_terminus/6'>N terminus stabilization with residues</scene>