Sandbox Reserved 1677: Difference between revisions
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<scene name='87/873239/Cartoon_view/5'>AldC's secondary structure</scene> has two domains, hydrophobic and hydrophilic regions. | <scene name='87/873239/Cartoon_view/5'>AldC's secondary structure</scene> has two domains, hydrophobic and hydrophilic regions. | ||
The N-terminus of Aldc contains a central beta sheet surrounded by alpha helices which forms the NAD(H)-binding site. | The N-terminus of Aldc contains a central beta sheet surrounded by alpha helices which forms the NAD(H)-binding site. | ||
Additionally, around the C-terminus there is a mixture of alpha and beta domains which the cysteine residue and forms the aldehyde binding site. A small three stranded beta sheet domain facilitates aligomerization. | Additionally, around the C-terminus there is a mixture of alpha and beta domains which includes the cysteine residue and forms the aldehyde binding site. A small three stranded beta sheet domain facilitates aligomerization. There is an interdomain linker region that connects the N and C terminal domains of Aldc. | ||
There is an interdomain linker region that connects the N and C terminal domains of Aldc. | |||
<scene name='87/873239/Spacefill/1'>Space filling view</scene> shows how amino acids interacts with one another inside the protein. | <scene name='87/873239/Spacefill/1'>Space filling view</scene> shows how amino acids interacts with one another inside the protein. | ||
== Other important features == | == Other important features == | ||
The Rossmann fold of the NAD(H) binding domain provides extensive polar and apolar interactions that position the nicotinamide ring of NAD+ in proximity to the C291A point mutation. Its main function is to bind NAD+ cofactor and contribute to substrate binding. | The Rossmann fold of the NAD(H) binding domain provides extensive polar and apolar interactions that position the nicotinamide ring of NAD+ in proximity to the C291A point mutation. Its main function is to bind NAD+ cofactor and contribute to substrate binding. | ||
