Phosphoglucoisomerase: Difference between revisions

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation. A "hook" that can potentially be involved in the previously mentioned extracellular activities.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red for highly conserved regions - dark blue for variable reigions) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/2'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).