Sandbox Reserved 1072

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[[Image:NterminalLOOP.png|300 px|left|thumb|Interlocking Hook]]
[[Image:NterminalLOOP.png|300 px|left|thumb|Interlocking Hook]]
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===Active Site===

Revision as of 13:39, 24 March 2015

This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.
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Structure

Image:StructureWHOLE.png
Structure

Mycobacterium Tuberculosis Catalase Peroxidase (mtCP) is a homodimer with each monomer consisting of two domains. The overall structure is stabilized by 703 water molecules.

Monomer Structure

The two domains of each monomer are primarily alpha helical and have similar foldings. The similar foldings suggests that the monomer results from a gene duplication event; however, the C-terminal domain does not contain the heme b prosthetic group, while the N-terminal 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. This interlocking loop region is also found in similar conformations of other catalase peroxidase structures such as: hmCP and bpCP (ADD LINK TO THESE PROTEOPEDIA PAGES).

Image:NterminalLOOP.png
Interlocking Hook

Active Site

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