Sandbox Reserved 1805: Difference between revisions

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Amino acids involved in the catalytic triad for MqnA include N17, S86, and Y242. Other amino acids that help bind the main ligand through hydrophobic interactions include I13, N17, V18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, and Y242. A view of just the ligand is shown <scene name='95/954102/Ligand/1'>here.</scene>

== Structural highlights ==

In terms of secondary structure, MqnA has both alpha helices and beta sheets present. In this <scene name='95/954102/Secondary_structure/1'>image</scene>, alpha helices are shown in red and beta sheets are shown in yellow. In our enzyme, there are two distinct lobes. These lobes are connected by linkers. Connected to the linkers on either lobe are beta sheets, followed by alpha helices. In terms of <scene name='95/954102/~~Tertiary_structure~~/1'>tertiary ~~and quaternary~~ structure</scene>, we see two distinct lobes present in MqnA. In the image, it is clear just how much space is occupied by the atoms, making our catalytic triad tucked away and hidden. This demonstrates the importance of the venus flytrap fold that exposes our ligand for binding. Its change in conformation is absolutely vital for its function. The tertiary structure (folded protein structure) is held together by side chain interactions, such as that between SER108 and ARG111 on MqnA. The quaternary structure shows how closely packed the amino acids are, leaving little to no access without the venus flytrap fold.

In terms of secondary structure, MqnA has both alpha helices and beta sheets present. In this <scene name='95/954102/Secondary_structure/1'>image</scene>, alpha helices are shown in red and beta sheets are shown in yellow. In our enzyme, there are two distinct lobes. These lobes are connected by linkers. Connected to the linkers on either lobe are beta sheets, followed by alpha helices. In terms of <scene name='95/954102/Tertiary1/1'>tertiary structure</scene> and quaternary structure, we see two distinct lobes present in MqnA. In the image, it is clear just how much space is occupied by the atoms, making our catalytic triad tucked away and hidden. Apla helices are represented in pink, beta sheets are represented in yellow, and coils are represented in white. This demonstrates the importance of the venus flytrap fold that exposes our ligand for binding. Its change in conformation is absolutely vital for its function. The tertiary structure (folded protein structure) is held together by side chain interactions, such as that between SER108 and ARG111 on MqnA. The <scene name='95/954102/Tertiary_structure/1'>quaternary structure</scene> shows how closely packed the amino acids are, leaving little to no access without the venus flytrap fold.

Sandbox Reserved 1805: Difference between revisions

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@@ Line 15: / Line 15: @@
 Amino acids involved in the catalytic triad for MqnA include N17, S86, and Y242. Other amino acids that help bind the main ligand through hydrophobic interactions include I13, N17, V18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, and Y242. A view of just the ligand is shown <scene name='95/954102/Ligand/1'>here.</scene>
 == Structural highlights ==
-In terms of secondary structure, MqnA has both alpha helices and beta sheets present. In this <scene name='95/954102/Secondary_structure/1'>image</scene>, alpha helices are shown in red and beta sheets are shown in yellow. In our enzyme, there are two distinct lobes. These lobes are connected by linkers. Connected to the linkers on either lobe are beta sheets, followed by alpha helices. In terms of <scene name='95/954102/Tertiary_structure/1'>tertiary and quaternary structure</scene>, we see two distinct lobes present in MqnA. In the image, it is clear just how much space is occupied by the atoms, making our catalytic triad tucked away and hidden. This demonstrates the importance of the venus flytrap fold that exposes our ligand for binding. Its change in conformation is absolutely vital for its function. The tertiary structure (folded protein structure) is held together by side chain interactions, such as that between SER108 and ARG111 on MqnA. The quaternary structure shows how closely packed the amino acids are, leaving little to no access without the venus flytrap fold.
+In terms of secondary structure, MqnA has both alpha helices and beta sheets present. In this <scene name='95/954102/Secondary_structure/1'>image</scene>, alpha helices are shown in red and beta sheets are shown in yellow. In our enzyme, there are two distinct lobes. These lobes are connected by linkers. Connected to the linkers on either lobe are beta sheets, followed by alpha helices. In terms of <scene name='95/954102/Tertiary1/1'>tertiary structure</scene> and quaternary structure, we see two distinct lobes present in MqnA. In the image, it is clear just how much space is occupied by the atoms, making our catalytic triad tucked away and hidden. Apla helices are represented in pink, beta sheets are represented in yellow, and coils are represented in white. This demonstrates the importance of the venus flytrap fold that exposes our ligand for binding. Its change in conformation is absolutely vital for its function. The tertiary structure (folded protein structure) is held together by side chain interactions, such as that between SER108 and ARG111 on MqnA. The <scene name='95/954102/Tertiary_structure/1'>quaternary structure</scene> shows how closely packed the amino acids are, leaving little to no access without the venus flytrap fold.