Sandbox Reserved 782
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<Structure load='3ie7' size='500' frame='true' align='right' caption='Phosphofructokinase from Listeria' scene='Scene 1' /> | <Structure load='3ie7' size='500' frame='true' align='right' caption='Phosphofructokinase from Listeria' scene='Scene 1' /> | ||
==Phosphofructokinase== | ==Phosphofructokinase== | ||
| - | + | <scene name='56/563194/Phosphofructokinase_scene_1/1'>Phosphofructokinase</scene> is an enzyme that is involved in the process of glycolysis. The particular reaction that it carries out is the catalysis of fructose-6-phosphate to fructose-1,6- bisphosphate via phosphorylation. The phosphofructokinase that is discussed on this page comes from the microbe ''Listeria innocua''. At the center you can see that the phosphofructokinase is bound to a molecule of ATP. In addition, the three green balls represent the three Mg atoms, and the small grey and red group off to the side is the glycerol. | |
The secondary structure is comprised of <scene name='56/563194/Alpha_helices_and_beta_sheets/1'>10 alpha-helices and 14 beta-sheets</scene>. The alpha helices are in yellow and the beta sheets are in grey. | The secondary structure is comprised of <scene name='56/563194/Alpha_helices_and_beta_sheets/1'>10 alpha-helices and 14 beta-sheets</scene>. The alpha helices are in yellow and the beta sheets are in grey. | ||
Revision as of 18:20, 15 October 2013
| This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807. |
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Phosphofructokinase
is an enzyme that is involved in the process of glycolysis. The particular reaction that it carries out is the catalysis of fructose-6-phosphate to fructose-1,6- bisphosphate via phosphorylation. The phosphofructokinase that is discussed on this page comes from the microbe Listeria innocua. At the center you can see that the phosphofructokinase is bound to a molecule of ATP. In addition, the three green balls represent the three Mg atoms, and the small grey and red group off to the side is the glycerol.
The secondary structure is comprised of . The alpha helices are in yellow and the beta sheets are in grey.
is a very important part of a proteins structure and stability. The hydrogen bonds of phosphofructokinase are designated by the orange dotted lines throughout the structure. Phosphofructokinase contains both anti-parallel and parallel sheets, which are identified by parallel hydrogen bonds and angled hydrogen bonds respectively.
One of the most important determining factors of protein structure lies in the interactions of the with the surrounding environment. The hydrophobic residues are designated with light green while the hydrophobic residues are shown in blue. As would be expected the majority of the hydrophobic residues are located at the center of the protein where they are shielded from the hydrophobic environment.
As previously mentioned, the hydrophobic interactions are critical in determining the protein structure. Here, the show that the water molecules predominantly gather around the outside of the protein, which is where most of the hydrophilic residues lie.
Looking at this phosphofructokinase you can see that the (represented in yellow) are lysine, arginine, histidine, and aspartic acid. These particular residues would be expected because they are all charged and polar, which would be ideal for interacting with glycerol (green) which is a polar molecule. In addition, the program did not specify any residues that interact with the ATP molecule (in pink).
Taking a further look into the active site of the protein, one can see that phosphofructokinase contains (represented in pink), two glycines, one aspartic acid, and one alanine. This particular placement of catalytic residues is to be expected because it allows the catalytic residues to have direct contact with the ligand (the green ATP), thus enabling the reaction to proceed at a faster rate via a catalytic mechanism.
