Sandbox Reserved 780
From Proteopedia
(→<scene name='56/563192/Fumarase_dimer/1'>Fumarase</scene>) |
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<Structure load='1FUO' size='500' frame='true' align='right' caption='Fumarase Dimer' scene='Insert optional scene name here' /> | <Structure load='1FUO' size='500' frame='true' align='right' caption='Fumarase Dimer' scene='Insert optional scene name here' /> | ||
==<scene name='56/563192/Fumarase_dimer/1'>Fumarase</scene>== | ==<scene name='56/563192/Fumarase_dimer/1'>Fumarase</scene>== | ||
| - | This is <scene name='56/563192/Fumarase_dimer/1'>fumarase</scene>. Fumarase is an enzyme of the citric acid cycle or Kreb's cycle. The function of fumarase is to stereospecifically convert fumarate into L-malate. This specific image (1FUO) is of Fumarase C from E. Coli. It is a dimer bound with 2 ligands; 2 citrate molecules and 2 malate molecules. The two citrate molecules are the two center <scene name='56/563192/Fumarase_ligandfocus/3'>ligands</scene> and the malate molecules are the outer two ligands shown. | + | This is <scene name='56/563192/Fumarase_dimer/1'>fumarase</scene>. Fumarase is an enzyme of the citric acid cycle or Kreb's cycle. The function of fumarase is to stereospecifically convert fumarate into L-malate. This specific image (1FUO) is of Fumarase C from E. Coli. It is a dimer bound with 2 ligands; 2 citrate molecules and 2 malate molecules. The two citrate molecules are the two center <scene name='56/563192/Fumarase_ligandfocus/3'>ligands</scene> and the malate molecules are the outer two ligands shown. The fumarate/L-malate conversion is reversible. |
| - | <scene name='56/563192/Fumarase_helix/1'>α-helicies</scene> | + | |
| - | <scene name='56/563192/Fumarase_sheet/1'>β- | + | A moajority of fumarase's secondary structure is composed of <scene name='56/563192/Fumarase_helix/1'>α-helicies</scene> shown in blue. The longer α-helicies are grouped together and appear to form short coiled coils which compse the mid section of the enzyme's structure. Fumarase contains 3 small sections of <scene name='56/563192/Fumarase_sheet/1'>β-sheets</scene>, each consisting of two strands in anti-parallel allignment connected by a short random coil. |
<scene name='56/563192/Fumarase_hbond/2'>Hydrogen Bonding</scene> | <scene name='56/563192/Fumarase_hbond/2'>Hydrogen Bonding</scene> | ||
<scene name='56/563192/Fumarase_hydrophilic0trans/1'>hydrophobic residues</scene> | <scene name='56/563192/Fumarase_hydrophilic0trans/1'>hydrophobic residues</scene> | ||
Revision as of 07:32, 18 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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This is . Fumarase is an enzyme of the citric acid cycle or Kreb's cycle. The function of fumarase is to stereospecifically convert fumarate into L-malate. This specific image (1FUO) is of Fumarase C from E. Coli. It is a dimer bound with 2 ligands; 2 citrate molecules and 2 malate molecules. The two citrate molecules are the two center and the malate molecules are the outer two ligands shown. The fumarate/L-malate conversion is reversible.
A moajority of fumarase's secondary structure is composed of shown in blue. The longer α-helicies are grouped together and appear to form short coiled coils which compse the mid section of the enzyme's structure. Fumarase contains 3 small sections of , each consisting of two strands in anti-parallel allignment connected by a short random coil.
