1ad4: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='1ad4' size='340' side='right'caption='[[1ad4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ad4]] is a 2 chain structure with 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=1AD4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AD4 FirstGlance]. <br>
+<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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
+</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>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ad4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ad4 OCA], [http://pdbe.org/1ad4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ad4 RCSB], [http://www.ebi.ac.uk/pdbsum/1ad4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ad4 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=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>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/DHPS_STAAU DHPS_STAAU]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 18: / Line 20: @@
 </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].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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:9149138<ref>PMID:9149138</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1ad4" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Dihydropteroate synthase|Dihydropteroate synthase]]
+*[[Dihydropteroate synthase 3D structures|Dihydropteroate synthase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Dihydropteroate synthase]]
 [[Category: Large Structures]]
 [[Category: Staphylococcus aureus]]
-[[Category: Kostrewa, D]]
+[[Category: Kostrewa D]]
-[[Category: Oefner, C]]
+[[Category: Oefner C]]
-[[Category: Dihydropteroate synthetase]]
-[[Category: Synthetase]]
-[[Category: Transferase]]