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.
Nolasco
Diego O
DO
Departamento de Física, UNESP, São José do Rio Preto, SP 15054-000, Brazil.
Canduri
Fernanda
F
Pereira
José H
JH
Cortinóz
Janaina R
JR
Palma
Mário S
MS
Oliveira
Jaim S
JS
Basso
Luiz A
LA
de Azevedo
Walter F
WF
Santos
Diógenes S
DS
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