2dhn
From Proteopedia
(Difference between revisions)
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<StructureSection load='2dhn' size='340' side='right'caption='[[2dhn]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2dhn' size='340' side='right'caption='[[2dhn]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2dhn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2dhn]] 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=2DHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DHN FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PH2:2-AMINO-6-HYDROXYMETHYL-7,8-DIHYDRO-3H-PTERIDIN-4-ONE'>PH2</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=2dhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dhn OCA], [https://pdbe.org/2dhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dhn RCSB], [https://www.ebi.ac.uk/pdbsum/2dhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dhn 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=2dhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dhn OCA], [https://pdbe.org/2dhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dhn RCSB], [https://www.ebi.ac.uk/pdbsum/2dhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dhn 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. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=2dhn ConSurf]. | </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=2dhn ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Dihydroneopterin aldolase catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin during the de novo synthesis of folic acid from guanosine triphosphate. The gene encoding the dihydroneopterin aldolase from S. aureus has been cloned, sequenced and expressed in Escherichia coli. The protein has been purified for biochemical characterization and its X-ray structure determined at 1.65 A resolution. The protein forms an octamer of 110,000 Mr molecular weight. Four molecules assemble into a ring, and two rings come together to give a cylinder with a hole of at least 13 A diameter. The structure of the binary complex with the product 6-hydroxymethyl-7,8-dihydropterin has defined the location of the active site. The structural information and results of site directed mutagenesis allow an enzyme reaction mechanism to be proposed. | ||
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| - | Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus.,Hennig M, D'Arcy A, Hampele IC, Page MG, Oefner C, Dale GE Nat Struct Biol. 1998 May;5(5):357-62. PMID:9586996<ref>PMID:9586996</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2dhn" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Aldolase 3D structures|Aldolase 3D structures]] | *[[Aldolase 3D structures|Aldolase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Arcy | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Dale | + | [[Category: D'Arcy A]] |
| - | [[Category: Hampele | + | [[Category: Dale G]] |
| - | [[Category: Hennig | + | [[Category: Hampele IC]] |
| - | [[Category: Oefner | + | [[Category: Hennig M]] |
| - | [[Category: Page | + | [[Category: Oefner CH]] |
| - | + | [[Category: Page MGP]] | |
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Current revision
COMPLEX OF 7,8-DIHYDRONEOPTERIN ALDOLASE FROM STAPHYLOCOCCUS AUREUS WITH 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN AT 2.2 A RESOLUTION
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