Sandbox Reserved 310: Difference between revisions

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Each monomer is comprised of 5 <scene name='Sandbox_Reserved_310/B-sheets/1'>β-strands</scene> and 4<scene name='Sandbox_Reserved_310/A_helices/2'>α-helices</scene> 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.

The isoalloxazine ring of FAD is located between α1 and α2 of the BLUF domain, between two highly conserved hydrophobic residues: Ile24 and Ile66<ref name="one" />. FAD forms hydrogen bonds with the following amino acid residues: Asn21, Asn32, Gln50, Arg65 and Asp69<ref name="one" />. More specifically, the side chain of Asn31 binds to O2 of FAD and Asn32 binds to N3 and O4 of FAD. The guanido group of Arg65 contributes to a network between FAD and the apo protein. The amide N of the Gln50 sidechain interacts with N5 and O4 of FAD through hydrogen bonding, while the amide O of the sidechain is closely linked with the hydroxyl oxygen of the highly conserved Tyr8 residue, forming a FAD-Gln50-Tyr8 network<ref name="one" />. This conserved Tyr8 residue is the only residue that has been shown to be essential for light reaction in the BLUF domain containing AppA and Slr1694 proteins<ref name ="seven">PMID: 17042486</ref>.

The isoalloxazine ring of FAD is located between <scene name='Sandbox_Reserved_310/Fad_interactions/1'>α1 and α2</scene> of the BLUF domain, between two highly conserved hydrophobic residues: Ile24 and Ile66<ref name="one" />. FAD forms hydrogen bonds with the following amino acid residues: Asn21, Asn32, Gln50, Arg65 and Asp69<ref name="one" />. More specifically, the side chain of Asn31 binds to O2 of FAD and Asn32 binds to N3 and O4 of FAD. The guanido group of Arg65 contributes to a network between FAD and the apo protein. The amide N of the Gln50 sidechain interacts with N5 and O4 of FAD through hydrogen bonding, while the amide O of the sidechain is closely linked with the hydroxyl oxygen of the highly conserved Tyr8 residue, forming a FAD-Gln50-Tyr8 network<ref name="one" />. This conserved Tyr8 residue is the only residue that has been shown to be essential for light reaction in the BLUF domain containing AppA and Slr1694 proteins<ref name ="seven">PMID: 17042486</ref>.

==Further Analyses==

Sandbox Reserved 310: Difference between revisions

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 Each monomer is comprised of 5 <scene name='Sandbox_Reserved_310/B-sheets/1'>β-strands</scene> and 4<scene name='Sandbox_Reserved_310/A_helices/2'>α-helices</scene> 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.
-The isoalloxazine ring of FAD is located between α1 and α2 of the BLUF domain, between two highly conserved hydrophobic residues: Ile24 and Ile66<ref name="one" />. FAD forms hydrogen bonds with the following amino acid residues: Asn21, Asn32, Gln50, Arg65 and Asp69<ref name="one" />. More specifically, the side chain of Asn31 binds to O2 of FAD and Asn32 binds to N3 and O4 of FAD. The guanido group of Arg65 contributes to a network between FAD and the apo protein. The amide N of the Gln50 sidechain interacts with N5 and O4 of FAD through hydrogen bonding, while the amide O of the sidechain is closely linked with the hydroxyl oxygen of the highly conserved Tyr8 residue, forming a FAD-Gln50-Tyr8 network<ref name="one" />. This conserved Tyr8 residue is the only residue that has been shown to be essential for light reaction in the BLUF domain containing AppA and Slr1694 proteins<ref name ="seven">PMID: 17042486</ref>.
+The isoalloxazine ring of FAD is located between <scene name='Sandbox_Reserved_310/Fad_interactions/1'>α1 and α2</scene> of the BLUF domain, between two highly conserved hydrophobic residues: Ile24 and Ile66<ref name="one" />. FAD forms hydrogen bonds with the following amino acid residues: Asn21, Asn32, Gln50, Arg65 and Asp69<ref name="one" />. More specifically, the side chain of Asn31 binds to O2 of FAD and Asn32 binds to N3 and O4 of FAD. The guanido group of Arg65 contributes to a network between FAD and the apo protein. The amide N of the Gln50 sidechain interacts with N5 and O4 of FAD through hydrogen bonding, while the amide O of the sidechain is closely linked with the hydroxyl oxygen of the highly conserved Tyr8 residue, forming a FAD-Gln50-Tyr8 network<ref name="one" />. This conserved Tyr8 residue is the only residue that has been shown to be essential for light reaction in the BLUF domain containing AppA and Slr1694 proteins<ref name ="seven">PMID: 17042486</ref>.
 ==Further Analyses==