Sandbox Reserved 1072
From Proteopedia
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''Mycobacterium Tuberculosis'' Catalase Peroxidase (''mt''CP) is a [http://en.wikipedia.org/wiki/Protein_dimer homodimer] with each monomer consisting of two [http://en.wikipedia.org/wiki/Protein_domain domains]. The overall structure is stabilized by 703 water molecules. | ''Mycobacterium Tuberculosis'' Catalase Peroxidase (''mt''CP) is a [http://en.wikipedia.org/wiki/Protein_dimer homodimer] with each monomer consisting of two [http://en.wikipedia.org/wiki/Protein_domain domains]. The overall structure is stabilized by 703 water molecules. | ||
===Monomer Structure=== | ===Monomer Structure=== | ||
| - | The two 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 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 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: ''hm''CP and ''bp''CP (ADD LINK TO THESE PROTEOPEDIA PAGES). | + | The two 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 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 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. The N-terminal hook 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: ''hm''CP and ''bp''CP (ADD LINK TO THESE PROTEOPEDIA PAGES). |
[[Image:NterminalLOOP.png|300 px|left|thumb|Interlocking Hook]] | [[Image:NterminalLOOP.png|300 px|left|thumb|Interlocking Hook]] | ||
===Active Site=== | ===Active Site=== | ||
Revision as of 13:42, 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
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. The N-terminal hook 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: hmCP and bpCP (ADD LINK TO THESE PROTEOPEDIA PAGES).
