2nm2: Difference between revisions

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==Overview==

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.

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 Structure==

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[[Category: x-ray crystallography]]

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 ==Overview==
-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.
+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 Structure==
@@ Line 29: / Line 29: @@
 [[Category: x-ray crystallography]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:46:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:08:25 2008''