Folylpolyglutamate synthase: Difference between revisions

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Michal Harel, Jaime Prilusky, Alexander Berchansky, Joel L. Sussman, Karsten Theis

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 ==Structure==
 <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/2'>conformational change</scene> into the active form. In the <scene name='74/748269/Glu/1'>Yersinia pestis structure</scene> 3qcz, glutamate and ATP are bound but the folate binding site is empty.
+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/3'>conformational change</scene> into the active form.
+{{Template:Button Toggle Animation2}}
+In the <scene name='74/748269/Glu/1'>Yersinia pestis structure</scene> 3qcz, glutamate and ATP are bound but the folate binding site is empty.
 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>. Water molecules shown as red spheres.