Structure of N5-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis.

نویسندگان

  • Micheal L Tuntland
  • Michael E Johnson
  • L W-M Fung
  • Bernard D Santarsiero
چکیده

The apo structure of N5-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis (baPurK) with Mg2+ in the active site is reported at 1.96 Å resolution. PurK is an enzyme in the purine-biosynthetic pathway, unique to prokaryotes, that converts 5-aminoimidazole ribonucleotide to N5-carboxyaminoimidazole ribonucleotide and has been suggested as a potential antimicrobial drug target. Two interesting features of baPurK are a flexible B-loop (residues 149/150-157) that is in close contact with the active site and the binding of Mg2+ to the active site without additional ligands.

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عنوان ژورنال:
  • Acta crystallographica. Section D, Biological crystallography

دوره 67 Pt 10  شماره 

صفحات  -

تاریخ انتشار 2011