Sandbox 48

Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. spinqualitylabelsall models Adenylate Kinase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Adenylate Kinase Adenylate kinase (or ADK) is an enzyme known to catalyze the reversible interconversion of adenosine triphosphate (ATP) and adenosine monophosphate (AMP) to two molecules of adenosine diphosphate (ADP). Reaction Scheme: ATP + AMP ⇔ 2 ADP This enzyme is important for cellular energy homeostasis because the need for ADP. ADP is required for oxidative phosphorylation, an important step in multiple metabolic pathways. Secondary Structure & Hydrogen Bonds The structure of chain A in adenylate kinase demonstrates the types of secondary structure that make up the enzyme. The secondary structures of chain A of adenylate kinase includes alpha- helices (green), and beta sheets (blue). There are 12 total helices in the enzyme, and 2 types of beta sheets, a parallel with 5 strands and an antiparallel with 2 strands. The location of the hydrogen bonds (black) within the secondary structure demonstrates how the alpha-helices and beta-sheets are hydrogen bonded. Hydrophobic and Hydrophilic Residues Within these structures the hydrophobic residues (purple) are located closest on the inside of the enzyme. The hydrophillic residues (green), which are those that are charged or polar, are on the outward face of the enzyme. Solvent Accessibility In the presence of solvent, the polar, hydrophilic residues of adenylate kinase interact with the molecules of solvent (purple). There is also solvent accessibility near the center of the molecule at the active site, and it is also accessible on the outward chains like the alpha helices. The ligand (green) is highlighted to show that the water molecules surround the ligand in the middle of the ligand, but not by the ends. Ligand Interaction There are charged residues that interact with the ligand, or make up the interaction site. The positively charged (blue) residues of the enzyme, which would include arginine (R123, R156, R167) and lysine (K13) interact with the negatively charged (red) residues of the ligand. There are also negatively charged portions of the active site, such as aspartic acid (D158, D159) that will interact with positively charged residues of the ligand. The ligand pictured is the inhibitory, non-hydrolyzable version of a substrate. It is similar in structure to ATP, but at the end of the triphosphate there is another adenosine. This will stop the reaction, and will allow our enzyme's structure to be analyzed in presence of a substrate.