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1ad4

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(New page: 200px<br /><applet load="1ad4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ad4, resolution 2.4&Aring;" /> '''DIHYDROPTEROATE SYNTH...)
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[[Image:1ad4.gif|left|200px]]<br /><applet load="1ad4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ad4, resolution 2.4&Aring;" />
 
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'''DIHYDROPTEROATE SYNTHETASE COMPLEXED WITH OH-CH2-PTERIN-PYROPHOSPHATE FROM STAPHYLOCOCCUS AUREUS'''<br />
 
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==Overview==
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==DIHYDROPTEROATE SYNTHETASE COMPLEXED WITH OH-CH2-PTERIN-PYROPHOSPHATE FROM STAPHYLOCOCCUS AUREUS==
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The gene encoding the dihydropteroate synthase of staphylococcus aureus, has been cloned, sequenced and expressed in Escherichia coli. The protein, has been purified for biochemical characterization and X-ray, crystallographic studies. The enzyme is a dimer in solution, has a steady, state kinetic mechanism that suggests random binding of the two substrates, and half-site reactivity. The crystal structure of apo-enzyme and a binary, complex with the substrate analogue hydroxymethylpterin pyrophosphate were, determined at 2.2 A and 2.4 A resolution, respectively. The enzyme belongs, to the group of "TIM-barrel" proteins and crystallizes as a, non-crystallographic dimer. Only one molecule of the substrate analogue, bound per dimer in the crystal. Sequencing of nine sulfonamide-resistant, clinical isolates has shown that as many as 14 residues could be involved, in resistance development. The residues are distributed over the surface, of the protein, which defies a simple interpretation of their roles in, resistance. Nevertheless, the three-dimensional structure of the substrate, analogue binary complex could give important insight into the molecular, mechanism of this enzyme.
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<StructureSection load='1ad4' size='340' side='right'caption='[[1ad4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ad4]] is a 2 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=1AD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AD4 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HH2:6-HYDROXYMETHYLPTERIN-DIPHOSPHATE'>HH2</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ad4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ad4 OCA], [https://pdbe.org/1ad4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ad4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ad4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ad4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DHPS_STAAU DHPS_STAAU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ad/1ad4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1ad4 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1AD4 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 MN, K and HH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydropteroate_synthase Dihydropteroate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.15 2.5.1.15] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AD4 OCA].
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*[[Dihydropteroate synthase 3D structures|Dihydropteroate synthase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure and function of the dihydropteroate synthase from Staphylococcus aureus., Hampele IC, D'Arcy A, Dale GE, Kostrewa D, Nielsen J, Oefner C, Page MG, Schonfeld HJ, Stuber D, Then RL, J Mol Biol. 1997 Apr 25;268(1):21-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9149138 9149138]
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[[Category: Large Structures]]
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[[Category: Dihydropteroate synthase]]
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[[Category: Single protein]]
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[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Kostrewa, D.]]
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[[Category: Kostrewa D]]
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[[Category: Oefner, C.]]
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[[Category: Oefner C]]
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[[Category: HH2]]
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[[Category: K]]
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[[Category: MN]]
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[[Category: dihydropteroate synthetase]]
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[[Category: synthetase]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:46:02 2007''
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Current revision

DIHYDROPTEROATE SYNTHETASE COMPLEXED WITH OH-CH2-PTERIN-PYROPHOSPHATE FROM STAPHYLOCOCCUS AUREUS

PDB ID 1ad4

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