User:Adam Mirando/Sandbox 1: Difference between revisions

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Bovine xanthine dehydrogenase has the overall dimensions 155 Ǻ x 90 Ǻ x 70 Ǻ in its dimeric form and 100 Ǻ x 90 Ǻ x 70 Ǻ for the individual protomers. The overall structure of the enzyme can be categorized into three key domains. The <scene name='User:Adam_Mirando/Sandbox_1/Xdh_domain/3'>N-terminal domain</scene> (green, residues 1- 165) harbors the two [http://en.wikipedia.org/wiki/Iron-sulfur_cluster Fe-S clusters] (shown in yellow). The second, <scene name='User:Adam_Mirando/Sandbox_1/Xdh_domain/3'>middle domain</scene> (blue, residues 226-531) contains the FAD domain (shown in orange) and the NAD+/O2 binding site. The <scene name='User:Adam_Mirando/Sandbox_1/Xdh_domain/3'>C-terminal domain</scene> (purple, residues 590-1332) contains the [http://en.wikipedia.org/wiki/Molybdopterin molybdopterin] cofactor (shown in red) and is positioned close to the interface between the other two domains. This structure allows for interactions between co-factors of the same ~~[http://en.wikipedia.org/wiki/Protomer~~ protomer]. However, closest distance of co-factors between the two subunits is greater than 50 Ǻ, suggesting that the two subunits do not cross communicate <ref name="structure">PMID:11005854</ref>.

Bovine xanthine dehydrogenase has the overall dimensions 155 Ǻ x 90 Ǻ x 70 Ǻ in its dimeric form and 100 Ǻ x 90 Ǻ x 70 Ǻ for the individual [http://en.wikipedia.org/wiki/Protomer protomers]. The overall structure of the enzyme can be categorized into three key domains. The <scene name='User:Adam_Mirando/Sandbox_1/Xdh_domain/3'>N-terminal domain</scene> (green, residues 1- 165) harbors the two [http://en.wikipedia.org/wiki/Iron-sulfur_cluster Fe-S clusters] (shown in yellow). The second, <scene name='User:Adam_Mirando/Sandbox_1/Xdh_domain/3'>middle domain</scene> (blue, residues 226-531) contains the FAD domain (shown in orange) and the NAD+/O2 binding site. The <scene name='User:Adam_Mirando/Sandbox_1/Xdh_domain/3'>C-terminal domain</scene> (purple, residues 590-1332) contains the [http://en.wikipedia.org/wiki/Molybdopterin molybdopterin] cofactor (shown in red) and is positioned close to the interface between the other two domains. This structure allows for interactions between co-factors of the same protomer. However, closest distance of co-factors between the two subunits is greater than 50 Ǻ, suggesting that the two subunits do not cross communicate <ref name="structure">PMID:11005854</ref>.

Revision as of 07:10, 29 April 2010 view source Adam Mirando (talk \| contribs) 101 edits No edit summary ← Older edit		Revision as of 07:15, 29 April 2010 view source Adam Mirando (talk \| contribs) 101 edits No edit summary Newer edit →
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	<applet load='1FO4' size='300' frame='true' align='right' caption='Bovine Milk Xanthine Dehydrogenase' />		<applet load='1FO4' size='300' frame='true' align='right' caption='Bovine Milk Xanthine Dehydrogenase' />
	Bovine xanthine dehydrogenase has the overall dimensions 155 Ǻ x 90 Ǻ x 70 Ǻ in its dimeric form and 100 Ǻ x 90 Ǻ x 70 Ǻ for the individual protomers. The overall structure of the enzyme can be categorized into three key domains. The <scene name='User:Adam_Mirando/Sandbox_1/Xdh_domain/3'>N-terminal domain</scene> (green, residues 1- 165) harbors the two [http://en.wikipedia.org/wiki/Iron-sulfur_cluster Fe-S clusters] (shown in yellow). The second, <scene name='User:Adam_Mirando/Sandbox_1/Xdh_domain/3'>middle domain</scene> (blue, residues 226-531) contains the FAD domain (shown in orange) and the NAD<sup>+</sup>/O<sub>2</sub> binding site. The <scene name='User:Adam_Mirando/Sandbox_1/Xdh_domain/3'>C-terminal domain</scene> (purple, residues 590-1332) contains the [http://en.wikipedia.org/wiki/Molybdopterin molybdopterin] cofactor (shown in red) and is positioned close to the interface between the other two domains. This structure allows for interactions between co-factors of the same ~~[http://en.wikipedia.org/wiki/Protomer~~ protomer]. However, closest distance of co-factors between the two subunits is greater than 50 Ǻ, suggesting that the two subunits do not cross communicate <ref name="structure">PMID:11005854</ref>.		Bovine xanthine dehydrogenase has the overall dimensions 155 Ǻ x 90 Ǻ x 70 Ǻ in its dimeric form and 100 Ǻ x 90 Ǻ x 70 Ǻ for the individual [http://en.wikipedia.org/wiki/Protomer protomers]. The overall structure of the enzyme can be categorized into three key domains. The <scene name='User:Adam_Mirando/Sandbox_1/Xdh_domain/3'>N-terminal domain</scene> (green, residues 1- 165) harbors the two [http://en.wikipedia.org/wiki/Iron-sulfur_cluster Fe-S clusters] (shown in yellow). The second, <scene name='User:Adam_Mirando/Sandbox_1/Xdh_domain/3'>middle domain</scene> (blue, residues 226-531) contains the FAD domain (shown in orange) and the NAD<sup>+</sup>/O<sub>2</sub> binding site. The <scene name='User:Adam_Mirando/Sandbox_1/Xdh_domain/3'>C-terminal domain</scene> (purple, residues 590-1332) contains the [http://en.wikipedia.org/wiki/Molybdopterin molybdopterin] cofactor (shown in red) and is positioned close to the interface between the other two domains. This structure allows for interactions between co-factors of the same protomer. However, closest distance of co-factors between the two subunits is greater than 50 Ǻ, suggesting that the two subunits do not cross communicate <ref name="structure">PMID:11005854</ref>.