Folylpolyglutamate synthase: Difference between revisions

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<StructureSection load='' size='400' side='right' caption='Folylpolyglutamate synthase complex with AMPPCP and Co+2 ion (pink) (PDB code [[2vor]])' scene='74/748269/Cv/1'>
<StructureSection load='' size='400' side='right' caption='Folylpolyglutamate synthase complex with AMPPCP and Co+2 ion (pink) (PDB code [[2vor]])' scene='74/748269/Cv/1'>


FPGS binds to ATP, glutamate and folate (DHF or THF). Once folate is bound, the enzyme undergoes a conformational change 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.
FPGS binds to ATP, glutamate and folate (DHF or THF). Once <scene name='74/748269/Folate/1'>folate is bound</scene>, the enzyme undergoes a conformational change 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.


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/5'>contains the nucleotide and a divalent ion</scene><ref>PMID:18566510</ref>. Water molecules shown as red spheres.
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/5'>contains the nucleotide and a divalent ion</scene><ref>PMID:18566510</ref>. Water molecules shown as red spheres.

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