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| | <StructureSection load='1tx0' size='340' side='right'caption='[[1tx0]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='1tx0' size='340' side='right'caption='[[1tx0]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1tx0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis_a2012 Bacillus anthracis a2012]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TX0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TX0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1tx0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_str._A2012 Bacillus anthracis str. A2012]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TX0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PT1:PTEROIC+ACID'>PT1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tws|1tws]], [[1tww|1tww]], [[1twz|1twz]], [[1tx2|1tx2]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PT1:PTEROIC+ACID'>PT1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=191218 Bacillus anthracis A2012])</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=1tx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tx0 OCA], [https://pdbe.org/1tx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tx0 RCSB], [https://www.ebi.ac.uk/pdbsum/1tx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tx0 ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1tx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tx0 OCA], [http://pdbe.org/1tx0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tx0 RCSB], [http://www.ebi.ac.uk/pdbsum/1tx0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tx0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q81VW8_BACAN Q81VW8_BACAN] |
| | == 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: Bacillus anthracis a2012]] | + | [[Category: Bacillus anthracis str. A2012]] |
| - | [[Category: Dihydropteroate synthase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Babaoglu, K]] | + | [[Category: Babaoglu K]] |
| - | [[Category: Lee, R E]] | + | [[Category: Lee RE]] |
| - | [[Category: Qi, J]] | + | [[Category: Qi J]] |
| - | [[Category: White, S W]] | + | [[Category: White SW]] |
| - | [[Category: Anthracis]]
| + | |
| - | [[Category: Dihydropteroate]]
| + | |
| - | [[Category: Folate biosynthesis]]
| + | |
| - | [[Category: Pterine]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q81VW8_BACAN
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
Dihydropterate synthase (DHPS) is the target for the sulfonamide class of antibiotics, but increasing resistance has encouraged the development of new therapeutic agents against this enzyme. One approach is to identify molecules that occupy the pterin binding pocket which is distinct from the pABA binding pocket that binds sulfonamides. Toward this goal, we present five crystal structures of DHPS from Bacillus anthracis, a well-documented bioterrorism agent. Three DHPS structures are already known, but our B. anthracis structures provide new insights into the enzyme mechanism. We show how an arginine side chain mimics the pterin ring in binding within the pterin binding pocket. The structures of two substrate analog complexes and the first structure of a DHPS-product complex offer new insights into the catalytic mechanism and the architecture of the pABA binding pocket. Finally, as an initial step in the development of pterin-based inhibitors, we present the structure of DHPS complexed with 5-nitro-6-methylamino-isocytosine.
Crystal structure of 7,8-dihydropteroate synthase from Bacillus anthracis: mechanism and novel inhibitor design.,Babaoglu K, Qi J, Lee RE, White SW Structure. 2004 Sep;12(9):1705-17. PMID:15341734[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Babaoglu K, Qi J, Lee RE, White SW. Crystal structure of 7,8-dihydropteroate synthase from Bacillus anthracis: mechanism and novel inhibitor design. Structure. 2004 Sep;12(9):1705-17. PMID:15341734 doi:10.1016/j.str.2004.07.011
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