Folylpolyglutamate synthase: Difference between revisions
| Line 11: | Line 11: | ||
==Structure== | ==Structure== | ||
<StructureSection load='' size='400' side='right' caption='' scene='74/748269/Cv/7'> | <StructureSection load='' size='400' side='right' caption='' scene='74/748269/Cv/7'> | ||
Folylpolyglutamate synthase is a single subunit enzyme with two domains (reload <scene name='74/748269/Cv/7'>initial scene</scene>). The three substrates (folate, ATP, glutamate) bind on the same face in a <scene name='74/748269/Conserved/1'>highly conserved patch</scene> near the domain boundary. FPGS binds to ATP, glutamate and folate (THF-(glu)n). Once <scene name='74/748269/Folate/1'>folate is bound</scene>, the enzyme undergoes a <scene name='74/748269/Folate_binding/ | Folylpolyglutamate synthase is a single subunit enzyme with two domains (reload <scene name='74/748269/Cv/7'>initial scene</scene>). The three substrates (folate, ATP, glutamate) bind on the same face in a <scene name='74/748269/Conserved/1'>highly conserved patch</scene> near the domain boundary. FPGS binds to ATP, glutamate and folate (THF-(glu)n). Once <scene name='74/748269/Folate/1'>folate is bound</scene>, the enzyme undergoes a <scene name='74/748269/Folate_binding/4'>conformational change</scene> into the active form. | ||
{{Template:Button Toggle Animation2}} | {{Template:Button Toggle Animation2}} | ||