Sandbox Reserved 477: Difference between revisions

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X- ray crystallography used to determine the crystal structure of the enzyme at 2.60 Å for the resolution. Glyceraldehyde-3-Phosphate Dehydrogenase is a homotetramer and has chains of exactly the same sequence and structure. "Depending on the isoform of GAPDH, there are different numbers of secondary structures; however, the more common GAPDHs have 14 <scene name='Sandbox_Reserved_477/Helix/1'>helices</scene> and 13 <scene name='Sandbox_Reserved_477/Beta_sheet/1'>beta strands</scene>. Evolutionary change for GAPDH is very slow, so there is high sequence similarity between bacterial and eukaryotic GAPDHs. Though not shown, the residue Cysteine 139 is the active site at the C end of the alpha helix 138-153. In bacteria and eukaryotes, a His 176 is conserved. The histidine is believed to act as a base that extracts a proton from the Cys 139 during catalysis." <ref>Mogri, M. (2004). Glyceraldehyde 3-phosphate dehydrogenase from sulfolobus solfataricus. Retrieved from http://www.stanford.edu/~mmogri/bio/gapdh/evolution.html</ref>

"X- ray crystallography used to determine the crystal structure of the enzyme at 2.60 Å for the resolution." <ref>This will be the PDB</ref> Glyceraldehyde-3-Phosphate Dehydrogenase is a homotetramer and has chains of exactly the same sequence and structure. "Depending on the isoform of GAPDH, there are different numbers of secondary structures; however, the more common GAPDHs have 14 <scene name='Sandbox_Reserved_477/Helix/1'>helices</scene> and 13 <scene name='Sandbox_Reserved_477/Beta_sheet/1'>beta strands</scene>. Evolutionary change for GAPDH is very slow, so there is high sequence similarity between bacterial and eukaryotic GAPDHs. Though not shown, the residue Cysteine 139 is the active site at the C end of the alpha helix 138-153. In bacteria and eukaryotes, a His 176 is conserved. The histidine is believed to act as a base that extracts a proton from the Cys 139 during catalysis." <ref>Mogri, M. (2004). Glyceraldehyde 3-phosphate dehydrogenase from sulfolobus solfataricus. Retrieved from http://www.stanford.edu/~mmogri/bio/gapdh/evolution.html</ref>

NAD+ is the most common <scene name='Sandbox_Reserved_477/Ligand/1'>ligand</scene> for the binding of GAPDH. A ligand is a molecule that binds to a central atom to form a complex. NAD+ expresses negative cooperativity in relation to GAPDH; as NAD+ binds to the protein, the protein's affinity for the ligand decreases.

Sandbox Reserved 477: Difference between revisions

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-X- ray crystallography used to determine the crystal structure of the enzyme at 2.60 Å for the resolution. Glyceraldehyde-3-Phosphate Dehydrogenase is a homotetramer and has chains of exactly the same sequence and structure. "Depending on the isoform of GAPDH, there are different numbers of secondary structures; however, the more common GAPDHs have 14 <scene name='Sandbox_Reserved_477/Helix/1'>helices</scene> and 13 <scene name='Sandbox_Reserved_477/Beta_sheet/1'>beta strands</scene>. Evolutionary change for GAPDH is very slow, so there is high sequence similarity between bacterial and eukaryotic GAPDHs. Though not shown, the residue Cysteine 139 is the active site at the C end of the alpha helix 138-153. In bacteria and eukaryotes, a His 176 is conserved. The histidine is believed to act as a base that extracts a proton from the Cys 139 during catalysis." <ref>Mogri, M. (2004). Glyceraldehyde 3-phosphate dehydrogenase from sulfolobus solfataricus. Retrieved from http://www.stanford.edu/~mmogri/bio/gapdh/evolution.html</ref>
+"X- ray crystallography used to determine the crystal structure of the enzyme at 2.60 Å for the resolution." <ref>This will be the PDB</ref> Glyceraldehyde-3-Phosphate Dehydrogenase is a homotetramer and has chains of exactly the same sequence and structure. "Depending on the isoform of GAPDH, there are different numbers of secondary structures; however, the more common GAPDHs have 14 <scene name='Sandbox_Reserved_477/Helix/1'>helices</scene> and 13 <scene name='Sandbox_Reserved_477/Beta_sheet/1'>beta strands</scene>. Evolutionary change for GAPDH is very slow, so there is high sequence similarity between bacterial and eukaryotic GAPDHs. Though not shown, the residue Cysteine 139 is the active site at the C end of the alpha helix 138-153. In bacteria and eukaryotes, a His 176 is conserved. The histidine is believed to act as a base that extracts a proton from the Cys 139 during catalysis." <ref>Mogri, M. (2004). Glyceraldehyde 3-phosphate dehydrogenase from sulfolobus solfataricus. Retrieved from http://www.stanford.edu/~mmogri/bio/gapdh/evolution.html</ref>
 NAD+ is the most common <scene name='Sandbox_Reserved_477/Ligand/1'>ligand</scene> for the binding of GAPDH. A ligand is a molecule that binds to a central atom to form a complex. NAD+ expresses negative cooperativity in relation to GAPDH; as NAD+ binds to the protein, the protein's affinity for the ligand decreases.