2nm2
From Proteopedia
(Difference between revisions)
(9 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | {{Seed}} | ||
- | [[Image:2nm2.png|left|200px]] | ||
- | < | + | ==Crystal structure of dihydroneopterin aldolase from S. aureus in complex with (1S,2R)-neopterin at 1.50 Angstrom resolution== |
- | + | <StructureSection load='2nm2' size='340' side='right'caption='[[2nm2]], [[Resolution|resolution]] 1.70Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[2nm2]] is a 4 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=2NM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NM2 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | |
- | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NEU:L-NEOPTERIN'>NEU</scene></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=2nm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nm2 OCA], [https://pdbe.org/2nm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nm2 RCSB], [https://www.ebi.ac.uk/pdbsum/2nm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nm2 ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/FOLB_STAAU FOLB_STAAU] Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/2nm2_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2nm2 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:17331536</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 2nm2" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Aldolase 3D structures|Aldolase 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | [[Category: Large Structures]] |
- | + | ||
- | + | ||
- | == | + | |
- | < | + | |
- | [[Category: | + | |
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
- | [[Category: Blaszczyk | + | [[Category: Blaszczyk J]] |
- | [[Category: Ji | + | [[Category: Ji X]] |
- | [[Category: Yan | + | [[Category: Yan H]] |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + |
Current revision
Crystal structure of dihydroneopterin aldolase from S. aureus in complex with (1S,2R)-neopterin at 1.50 Angstrom resolution
|