1tx0: Difference between revisions

← Older edit

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1tx0.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1tx0", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_1tx0|  PDB=1tx0  |  SCENE=  }}
-'''Dihydropteroate Synthetase, With Bound Product Analogue Pteroic Acid, From Bacillus anthracis'''
+==Dihydropteroate Synthetase, With Bound Product Analogue Pteroic Acid, From Bacillus anthracis==
+<StructureSection load='1tx0' size='340' side='right'caption='[[1tx0]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</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='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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q81VW8_BACAN Q81VW8_BACAN]
+== 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/tx/1tx0_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=1tx0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-==Overview==
+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<ref>PMID:15341734</ref>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-TX0 is a [[Single protein]] structure of sequence from [http://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].
+</div>
+<div class="pdbe-citations 1tx0" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/15341734 15341734]
+*[[Dihydropteroate synthase 3D structures|Dihydropteroate synthase 3D structures]]
-[[Category: Bacillus anthracis str. a2012]]
+== References ==
-[[Category: Dihydropteroate synthase]]
+<references/>
-[[Category: Single protein]]
+__TOC__
-[[Category: Babaoglu, K.]]
+</StructureSection>
-[[Category: Lee, R E.]]
+[[Category: Bacillus anthracis str. A2012]]
-[[Category: Qi, J.]]
+[[Category: Large Structures]]
-[[Category: White, S W.]]
+[[Category: Babaoglu K]]
-[[Category: Anthracis]]
+[[Category: Lee RE]]
-[[Category: Dihydropteroate]]
+[[Category: Qi J]]
-[[Category: Folate biosynthesis]]
+[[Category: White SW]]
-[[Category: Pterine]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:28:22 2008''