Sandbox Reserved 1759: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major | The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid chains, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. | ||
.In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well | |||
MBD is ATP-independent but evolves from the ATP-dependent , The MBD enzymes ligand binding site overlaps with the ATP binding site of its homologous enzyme, DMD. | MBD is ATP-independent but evolves from the ATP-dependent , The MBD enzymes ligand binding site overlaps with the ATP binding site of its homologous enzyme, DMD. | ||
