ATP Phosphoribosyl Transferase: Difference between revisions

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<applet load='1z7n' size='350' frame='true' align='right' caption='ATP phosphoribosyltransferase regulatory subunit tetramer (grey, green, pink, yellow) with ATP phosphoribosyltransferase (magenta, cyan, red, gold) complex with substrate α-phosphoribosylpyrophosphoric acid (PRPP) and phosphate, [[1z7n]]' />
<applet load='1z7n' size='350' frame='true' align='right' caption='ATP phosphoribosyltransferase regulatory subunit tetramer (grey, green, pink, yellow) with ATP phosphoribosyltransferase (magenta, cyan, red, gold) complex with substrate α-phosphoribosylpyrophosphoric acid (PRPP) and phosphate, [[1z7n]]' />
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'''Structure of ATP-PRTase from ''Mycobacterium tuberculosis'''''<ref> Cho Y, Sharma, V and Sacchettini; (2003). Crystal structure of ATP phosphoribosyl transferase from ''Mycobacterium tuberculosis'', J. Biol. Chem. '''278''', 8333-8339 </ref>
=='''Structure of ATP-PRTase from ''Mycobacterium tuberculosis'''==''<ref> Cho Y, Sharma, V and Sacchettini; (2003). Crystal structure of ATP phosphoribosyl transferase from ''Mycobacterium tuberculosis'', J. Biol. Chem. '''278''', 8333-8339 </ref>


ATP-PRTase has three domains with an α/β fold. The C-terminal domain (domain 3), consisting of a beta sheet with four strands is flanked on one side of the sheet by two helices. The two N-terminal domains house the catalytic site in their interdomain region. Domain 1 has a central beta sheet with three helices around it whilst domain 2 has two  helices on each side of a sheet made up of four parallel strands and one anti parallel strand.  
ATP-PRTase has three domains with an α/β fold. The C-terminal domain (domain 3), consisting of a beta sheet with four strands is flanked on one side of the sheet by two helices. The two N-terminal domains house the catalytic site in their interdomain region. Domain 1 has a central beta sheet with three helices around it whilst domain 2 has two  helices on each side of a sheet made up of four parallel strands and one anti parallel strand.  

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Lawrence Sheringham Borketey, David Canner, Michal Harel, Alexander Berchansky