Crystallographic structure of PNP from Mycobacterium tuberculosis at 1.9A resolution.
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.
Departamento de Física, UNESP, São José do Rio Preto, SP 15054-000, Brazil.
Diego O
DO
Nolasco
Fernanda
F
Canduri
José H
JH
Pereira
Janaina R
JR
Cortinóz
Mário S
MS
Palma
Jaim S
JS
Oliveira
Luiz A
LA
Basso
Walter F
WF
de Azevedo
Diógenes S
DS
Santos
D001665:Binding Sites; D018360:Crystallography, X-Ray / Q000379:methods*; D019281:Dimerization; D015195:Drug Design; D008958:Models, Molecular; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D011487:Protein Conformation; D011683:Purine-Nucleoside Phosphorylase / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; D011683:Purine-Nucleoside Phosphorylase