Crystallographic and molecular dynamics simulation analysis of Escherichia coli dihydroneopterin aldolase.

ABSTRACT:

Background

Dihydroneopterin aldolase (DHNA) catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin and also the epimerization of DHNP to 7,8-dihydromonapterin. Previously, we determined the crystal structure of Staphylococcus aureus DHNA (SaDHNA) in complex with the substrate analogue neopterin (NP). We also showed that Escherichia coli DHNA (EcDHNA) and SaDHNA have significantly different binding and catalytic properties by biochemical analysis. On the basis of these structural and functional data, we proposed a catalytic mechanism involving two proton wires.

Results

To understand the structural basis for the biochemical differences and further investigate the catalytic mechanism of DHNA, we have determined the structure of EcDHNA complexed wi

SUBMITTER: Blaszczyk J 

PROVIDER: S-EPMC4176595 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature