3lrf: Difference between revisions

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-{{Seed}}
-[[Image:3lrf.jpg|left|200px]]
-<!--
+==Crystal structure of beta-ketoacyl synthase from brucella melitensis==
-The line below this paragraph, containing "STRUCTURE_3lrf", creates the "Structure Box" on the page.
+<StructureSection load='3lrf' size='340' side='right'caption='[[3lrf]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3lrf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_abortus_2308 Brucella abortus 2308]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LRF FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-{{STRUCTURE_3lrf|  PDB=3lrf  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lrf OCA], [https://pdbe.org/3lrf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lrf RCSB], [https://www.ebi.ac.uk/pdbsum/3lrf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lrf ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q2YQQ9_BRUA2 Q2YQQ9_BRUA2]
+== 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/lr/3lrf_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=3lrf ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The bacterial fatty acid pathway is essential for membrane synthesis and a range of other metabolic and cellular functions. The beta-ketoacyl-ACP synthases carry out the initial elongation reaction of this pathway, utilizing acetyl-CoA as a primer to elongate malonyl-ACP by two carbons, and subsequent elongation of the fatty acyl-ACP substrate by two carbons. Here we describe the structures of the beta-ketoacyl-ACP synthase I from Brucella melitensis in complex with platencin, 7-hydroxycoumarin, and (5-thiophen-2-ylisoxazol-3-yl)methanol. The enzyme is a dimer and based on structural and sequence conservation, harbors the same active site configuration as other beta-ketoacyl-ACP synthases. The platencin binding site overlaps with the fatty acyl compound supplied by ACP, while 7-hydroxyl-coumarin and (5-thiophen-2-ylisoxazol-3-yl)methanol bind at the secondary fatty acyl binding site. These high-resolution structures, ranging between 1.25 and 1.70 a resolution, provide a basis for in silico inhibitor screening and optimization, and can aid in rational drug design by revealing the high-resolution binding interfaces of molecules at the malonyl-ACP and acyl-ACP active sites.
-===Crystal structure of beta-ketoacyl synthase from brucella melitensis===
+Structural characterization of beta-ketoacyl ACP synthase I bound to platencin and fragment screening molecules at two substrate binding sites.,Patterson EI, Nanson JD, Abendroth J, Bryan C, Sankaran B, Myler PJ, Forwood JK Proteins. 2019 Jun 25. doi: 10.1002/prot.25765. PMID:31237717<ref>PMID:31237717</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-==About this Structure==
+</div>
-LRF is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brucella_abortus Brucella abortus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LRF OCA].
+<div class="pdbe-citations 3lrf" style="background-color:#fffaf0;"></div>
-[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
+== References ==
-[[Category: Brucella abortus]]
+<references/>
-[[Category: Abendroth, J.]]
+__TOC__
-[[Category: Edwards, T.]]
+</StructureSection>
-[[Category: SSGCID, Seattle Structural Genomics Center for Infectious Disease.]]
+[[Category: Brucella abortus 2308]]
-[[Category: Staker, B.]]
+[[Category: Large Structures]]
-[[Category: Acyltransferase]]
+[[Category: Abendroth J]]
-[[Category: Beta-ketoacyl synthase]]
+[[Category: Edwards T]]
-[[Category: Brucella melitensis]]
+[[Category: Staker B]]
-[[Category: Emerald biostructure]]
-[[Category: Niaid]]
-[[Category: Nih]]
-[[Category: Sbri]]
-[[Category: Seattle structural genomics center for infectious disease]]
-[[Category: Ssgcid]]
-[[Category: Structural genomic]]
-[[Category: Transferase]]
-[[Category: Uw]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 31 13:53:30 2010''