Crystallographic structure of PNP from Mycobacterium tuberculosis at 1.9A resolution

Biochem Biophys Res Commun. 2004 Nov 12;324(2):789-94. doi: 10.1016/j.bbrc.2004.09.137.

Abstract

Even being a bacterial purine nucleoside phosphorylase (PNP), which normally shows hexameric folding, the Mycobacterium tuberculosis PNP (MtPNP) resembles the mammalian trimeric structure. The crystal structure of the MtPNP apoenzyme was solved at 1.9 A resolution. The present work describes the first structure of MtPNP in complex with phosphate. In order to develop new insights into the rational drug design, conformational changes were profoundly analyzed and discussed. Comparisons over the binding sites were specially studied to improve the discussion about the selectivity of potential new drugs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Crystallography, X-Ray / methods*
  • Dimerization
  • Drug Design
  • Models, Molecular
  • Mycobacterium tuberculosis / enzymology*
  • Protein Conformation
  • Purine-Nucleoside Phosphorylase / chemistry*
  • Recombinant Proteins / chemistry

Substances

  • Recombinant Proteins
  • Purine-Nucleoside Phosphorylase