2nm3
Crystal structure of dihydroneopterin aldolase from S. aureus in complex with (1S,2S)-monapterin at 1.68 angstrom resolution
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OverviewOverview
Dihydroneopterin aldolase (DHNA) catalyzes the conversion of, 7,8-dihydroneopterin (DHNP) to 6-hydroxymethyl-7,8-dihydropterin (HP) and, the epimerization of DHNP to 7,8-dihydromonopterin (DHMP). Although, crystal structures of the enzyme from several microorganisms have been, reported, no structural information is available about the critical, interactions between DHNA and the trihydroxypropyl moiety of the, substrate, which undergoes bond cleavage and formation. Here, we present, the structures of Staphylococcus aureus DHNA (SaDHNA) in complex with, neopterin (NP, an analog of DHNP) and with monapterin (MP, an analog of, DHMP), filling the gap in the structural analysis of the enzyme. In, combination with previously reported SaDHNA structures in its ligand-free, form (PDB entry 1DHN) and in complex with HP (PDB entry 2DHN), four, snapshots for the catalytic center assembly along the reaction pathway can, be derived, advancing our knowledge about the molecular mechanism of, SaDHNA-catalyzed reactions. An additional step appears to be necessary for, the epimerization of DHMP to DHNP. Three active site residues (E22, K100, and Y54) function coordinately during catalysis: together, they organize, the catalytic center assembly, and individually, each plays a central role, at different stages of the catalytic cycle.
About this StructureAbout this Structure
2NM3 is a Single protein structure of sequence from Staphylococcus aureus with ACT and MPU as ligands. Active as Dihydroneopterin aldolase, with EC number 4.1.2.25 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for the aldolase and epimerase activities of Staphylococcus aureus dihydroneopterin aldolase., Blaszczyk J, Li Y, Gan J, Yan H, Ji X, J Mol Biol. 2007 Apr 20;368(1):161-9. Epub 2007 Feb 9. PMID:17331536
Page seeded by OCA on Wed Nov 21 12:47:49 2007