2O90

Atomic resolution crystal structure of E.coli dihydroneopterin aldolase in complex with neopterin

Summary for 2O90

Entry DOI	10.2210/pdb2o90/pdb
Related	1DHN 2DHN 2NM2 2NM3 2O9M 2OAK
Descriptor	Dihydroneopterin aldolase, L-NEOPTERIN (3 entities in total)
Functional Keywords	dihydroneopterin aldolase, dhna, neopterin, monapterin, 7, 8-dihydroneopterin, drug design, atomic resolution, lyase
Biological source	Escherichia coli
Total number of polymer chains	1
Total formula weight	13886.69
Authors	Blaszczyk, J.,Ji, X.,Yan, H. (deposition date: 2006-12-12, release date: 2007-12-25, Last modification date: 2023-08-30)
Primary citation	Blaszczyk, J.,Lu, Z.,Li, Y.,Yan, H.,Ji, X. Crystallographic and molecular dynamics simulation analysis of Escherichia coli dihydroneopterin aldolase. Cell Biosci, 4:52-52, 2014 Cited by PubMed Abstract: 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. PubMed: 25264482 DOI: 10.1186/2045-3701-4-52 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.07 Å)

Structure validation