2nm2

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[[Image:2nm2.jpg|left|200px]]<br /><applet load="2nm2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2nm2.jpg|left|200px]]
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caption="2nm2, resolution 1.70&Aring;" />
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'''Crystal structure of dihydroneopterin aldolase from S. aureus in complex with (1S,2R)-neopterin at 1.50 Angstrom resolution'''<br />
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{{Structure
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|PDB= 2nm2 |SIZE=350|CAPTION= <scene name='initialview01'>2nm2</scene>, resolution 1.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NEU:L-NEOPTERIN'>NEU</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Dihydroneopterin_aldolase Dihydroneopterin aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.25 4.1.2.25]
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|GENE= folB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
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}}
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'''Crystal structure of dihydroneopterin aldolase from S. aureus in complex with (1S,2R)-neopterin at 1.50 Angstrom resolution'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2NM2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=NEU:'>NEU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Dihydroneopterin_aldolase Dihydroneopterin aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.25 4.1.2.25] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NM2 OCA].
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2NM2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NM2 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17331536 17331536]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17331536 17331536]
[[Category: Dihydroneopterin aldolase]]
[[Category: Dihydroneopterin aldolase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: x-ray crystallography]]
[[Category: x-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:08:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:48:11 2008''

Revision as of 15:48, 20 March 2008


PDB ID 2nm2

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands:
Gene: folB (Staphylococcus aureus)
Activity: Dihydroneopterin aldolase, with EC number 4.1.2.25
Coordinates: save as pdb, mmCIF, xml



Crystal structure of dihydroneopterin aldolase from S. aureus in complex with (1S,2R)-neopterin at 1.50 Angstrom resolution


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.

About this Structure

2NM2 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

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

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