Sandbox Reserved 310: Difference between revisions
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==Domains== | ==Domains== | ||
[[Image:FADbonding.jpg|thumb|left|300px|Figure 1. The hydrogen bonds the FAD ligand forms with nearby amino acid residues.]] | [[Image:FADbonding.jpg|thumb|left|300px|Figure 1. The hydrogen bonds the FAD ligand forms with nearby amino acid residues.]] | ||
The BLUF domain is a <scene name='Sandbox_Reserved_310/ | The BLUF domain is a <scene name='Sandbox_Reserved_310/Decamer/1'>decamer</scene> with a molecular weight of approximately 160kDa<ref name="one" />. There are ten monomers observed in each asymmetric unit. The crystalline structure of the BLUF domain from the T110078 protein was solved by single isomorphous replacement (SIR) method using a mercury derivative. The double ringed decamer has a diameter of approximately 95Å, a thickness of 60Å and a central channel approximately 35Å in diameter<ref name="one" />. | ||
Each monomer is comprised of 5 β-strands and 4 α-helices in the order of β1α1β2β3α2β4β5α3α4. Specifically, the BLUF domain of the monomer contains β1α1β2β3α2β4β5, while the C-terminal domain contains α3α4<ref name="one" />. The C-terminal domain interacts with the end of the β-sheet of the neighbouring monomer. | Each monomer is comprised of 5 β-strands and 4 α-helices in the order of β1α1β2β3α2β4β5α3α4. Specifically, the BLUF domain of the monomer contains β1α1β2β3α2β4β5, while the C-terminal domain contains α3α4<ref name="one" />. The C-terminal domain interacts with the end of the β-sheet of the neighbouring monomer. | ||