PMID- 15474496
OWN - NLM
STAT- MEDLINE
DCOM- 20041220
LR  - 20061115
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 324
IP  - 2
DP  - 2004 Nov 12
TI  - Crystallographic structure of PNP from Mycobacterium tuberculosis at 1.9A 
      resolution.
PG  - 789-94
AB  - 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.
FAU - Nolasco, Diego O
AU  - Nolasco DO
AD  - Departamento de Fisica, UNESP, Sao Jose do Rio Preto, SP 15054-000, Brazil.
FAU - Canduri, Fernanda
AU  - Canduri F
FAU - Pereira, Jose H
AU  - Pereira JH
FAU - Cortinoz, Janaina R
AU  - Cortinoz JR
FAU - Palma, Mario S
AU  - Palma MS
FAU - Oliveira, Jaim S
AU  - Oliveira JS
FAU - Basso, Luiz A
AU  - Basso LA
FAU - de Azevedo, Walter F Jr
AU  - de Azevedo WF Jr
FAU - Santos, Diogenes S
AU  - Santos DS
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Recombinant Proteins)
RN  - EC 2.4.2.1 (Purine-Nucleoside Phosphorylase)
SB  - IM
MH  - Binding Sites
MH  - Crystallography, X-Ray/*methods
MH  - Dimerization
MH  - Drug Design
MH  - Models, Molecular
MH  - Mycobacterium tuberculosis/*enzymology
MH  - Protein Conformation
MH  - Purine-Nucleoside Phosphorylase/*chemistry
MH  - Recombinant Proteins/chemistry
EDAT- 2004/10/12 09:00
MHDA- 2004/12/21 09:00
CRDT- 2004/10/12 09:00
PHST- 2004/09/01 00:00 [received]
PHST- 2004/10/12 09:00 [pubmed]
PHST- 2004/12/21 09:00 [medline]
PHST- 2004/10/12 09:00 [entrez]
AID - S0006-291X(04)02135-7 [pii]
AID - 10.1016/j.bbrc.2004.09.137 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2004 Nov 12;324(2):789-94. doi: 
      10.1016/j.bbrc.2004.09.137.