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| | <StructureSection load='2nm3' size='340' side='right'caption='[[2nm3]], [[Resolution|resolution]] 1.68Å' scene=''> | | <StructureSection load='2nm3' size='340' side='right'caption='[[2nm3]], [[Resolution|resolution]] 1.68Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2nm3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NM3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2nm3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NM3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPU:D-MONAPTERIN'>MPU</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2nm2|2nm2]], [[1dhn|1dhn]], [[2dhn|2dhn]], [[1nbu|1nbu]], [[1rr5|1rr5]], [[1rri|1rri]], [[1rrw|1rrw]], [[1rry|1rry]], [[1rs2|1rs2]], [[1rs4|1rs4]], [[1rsd|1rsd]], [[1rsi|1rsi]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPU:D-MONAPTERIN'>MPU</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydroneopterin_aldolase Dihydroneopterin aldolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.25 4.1.2.25] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nm3 OCA], [https://pdbe.org/2nm3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nm3 RCSB], [https://www.ebi.ac.uk/pdbsum/2nm3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nm3 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nm3 OCA], [https://pdbe.org/2nm3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nm3 RCSB], [https://www.ebi.ac.uk/pdbsum/2nm3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nm3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FOLB_STAAU FOLB_STAAU]] Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
| + | [https://www.uniprot.org/uniprot/FOLB_STAAU FOLB_STAAU] Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dihydroneopterin aldolase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Blaszczyk, J]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Ji, X]] | + | [[Category: Blaszczyk J]] |
| - | [[Category: Yan, H]] | + | [[Category: Ji X]] |
| - | [[Category: 8-dihydromonapterin]] | + | [[Category: Yan H]] |
| - | [[Category: Dhna]]
| + | |
| - | [[Category: Drug design]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Monapterin]]
| + | |
| - | [[Category: Neopterin]]
| + | |
| - | [[Category: Substrate complex]]
| + | |
| Structural highlights
Function
FOLB_STAAU Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Blaszczyk J, Li Y, Gan J, Yan H, Ji X. Structural basis for the aldolase and epimerase activities of Staphylococcus aureus dihydroneopterin aldolase. J Mol Biol. 2007 Apr 20;368(1):161-9. Epub 2007 Feb 9. PMID:17331536 doi:10.1016/j.jmb.2007.02.009
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