2fus: Difference between revisions

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-{{Seed}}
-[[Image:2fus.png|left|200px]]
-<!--
+==MUTATIONS OF FUMARASE THAT DISTINGUISH BETWEEN THE ACTIVE SITE AND A NEARBY DICARBOXYLIC ACID BINDING SITE==
-The line below this paragraph, containing "STRUCTURE_2fus", creates the "Structure Box" on the page.
+<StructureSection load='2fus' size='340' side='right'caption='[[2fus]], [[Resolution|resolution]] 2.20&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'>[[2fus]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FUS 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]] 2.2&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
-{{STRUCTURE_2fus|  PDB=2fus  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fus OCA], [https://pdbe.org/2fus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fus RCSB], [https://www.ebi.ac.uk/pdbsum/2fus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fus ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FUMC_ECOLI FUMC_ECOLI] Catalyzes the reversible addition of water to fumarate to give L-malate.<ref>PMID:1917897</ref>
+== 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/fu/2fus_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=2fus ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Two mutant forms of fumarase C from E. coli have been made using PCR and recombinant DNA. The recombinant form of the protein included a histidine arm on the C-terminal facilitating purification. Based on earlier studies, two different carboxylic acid binding sites, labeled A- and B-, were observed in crystal structures of the wild type and inhibited forms of the enzyme. A histidine at each of the sites was mutated to an asparagine. H188N at the A-site resulted in a large decrease in specific activity, while the H129N mutation at the B-site had essentially no effect. From the results, we conclude that the A-site is indeed the active site, and a dual role for H188 as a potential catalytic base is proposed. Crystal structures of the two mutant proteins produced some unexpected results. Both mutations reduced the affinity for the carboxylic acids at their respective sites. The H129N mutant should be particularly useful in future kinetic studies because it sterically blocks the B-site with the carboxyamide of asparagine assuming the position of the ligand's carboxylate. In the H188N mutation at the active site, the new asparagine side chain still interacts with an active site water that appears to have moved slightly as a result of the mutation.
-===MUTATIONS OF FUMARASE THAT DISTINGUISH BETWEEN THE ACTIVE SITE AND A NEARBY DICARBOXYLIC ACID BINDING SITE===
+Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site.,Weaver T, Lees M, Banaszak L Protein Sci. 1997 Apr;6(4):834-42. PMID:9098893<ref>PMID:9098893</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2fus" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_9098893}}, adds the Publication Abstract to the page
+*[[Fumarase|Fumarase]]
-(as it appears on PubMed at http://www.pubmed.gov), where 9098893 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9098893}}
+__TOC__
+</StructureSection>
-==About this Structure==
-FUS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUS OCA].
-==Reference==
-Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site., Weaver T, Lees M, Banaszak L, Protein Sci. 1997 Apr;6(4):834-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9098893 9098893]
 [[Category: Escherichia coli]]
-[[Category: Fumarate hydratase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Banaszak LJ]]
-[[Category: Banaszak, L J.]]
+[[Category: Lees M]]
-[[Category: Lees, M.]]
+[[Category: Weaver TM]]
-[[Category: Weaver, T M.]]
-[[Category: Carbon oxygen lyase]]
-[[Category: Fumarate hydratase]]
-[[Category: Hydrolyase]]
-[[Category: Kreb's cycle enzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:06:41 2008''