Folylpolyglutamate synthase: Difference between revisions
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==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. Once <scene name='74/748269/Folate/ | 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. Once <scene name='74/748269/Folate/2'>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}} | ||
The <scene name='74/748269/Glu/ | The <scene name='74/748269/Glu/2'>Yersinia pestis structure</scene> 3qcz, shows glutamate bound near ATP while the folate binding site is empty. There is no structure where all three substrates are bound simultaneously yet. | ||
The nucleotide-binding pocket of FPGS occupies a <scene name='74/748269/Cv/4'>narrow channel between the N- and C-terminal domains</scene> of the protein and <scene name='74/748269/Cv/6'>contains the nucleotide and a divalent ion</scene><ref>PMID:18566510</ref>. | The nucleotide-binding pocket of FPGS occupies a <scene name='74/748269/Cv/4'>narrow channel between the N- and C-terminal domains</scene> of the protein and <scene name='74/748269/Cv/6'>contains the nucleotide and a divalent ion</scene><ref>PMID:18566510</ref>. | ||