2gzr: Difference between revisions

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OCA

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-[[Image:2gzr.gif|left|200px]]<br /><applet load="2gzr" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2gzr, resolution 2.3&Aring;" />
-'''Enterobactin and Salmochelin Hydrolase IroE'''<br />
-==Overview==
+==Enterobactin and Salmochelin Hydrolase IroE==
-The proliferation of many pathogenic bacteria is limited by the scarcity, of soluble iron in their environment. Many of these bacteria scavenge iron, by synthesizing and exporting small molecule siderophores that chelate, iron. Iron-bound siderophores are subsequently imported for metabolic, processing. Three related serine hydrolases have been characterized, biochemically in this pathway: Fes, IroD, and IroE. Here, we report the, crystal structure of IroE from uropathogenic Escherichia coli CFT073. The, native structure and a complex with diisopropyl fluorophosphonate (DFP, a, potent serine hydrolase inhibitor) were determined at 2.3 and 1.4 A, resolution, respectively. IroE has the typical alpha/beta-hydrolase fold, with an atypical catalytic dyad composed of Ser 189 and His 287. Mutation, of either residue was detrimental to catalysis. In addition, rather than, the typical oxyanion hole composed of backbone amides, IroE employs the, atypical guanidinium moiety of Arg 130. Asp 90 anchors Arg 130 in the, active site, and mutation of either residue was likewise detrimental to, catalysis. We also compare the structure of IroE to the structure of Fes, from Shigella flexneri (PDB entry 2B20). Both enzymes have similar active, sites, but Fes has an additional amino-terminal lid domain. These lid, domains are proposed to confer specificity to these related hydrolases.
+<StructureSection load='2gzr' size='340' side='right'caption='[[2gzr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2gzr]] is a 1 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=2GZR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GZR 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]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2gzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gzr OCA], [https://pdbe.org/2gzr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gzr RCSB], [https://www.ebi.ac.uk/pdbsum/2gzr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gzr ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q6KD95_ECOLX Q6KD95_ECOLX]
+== 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/gz/2gzr_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=2gzr ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The proliferation of many pathogenic bacteria is limited by the scarcity of soluble iron in their environment. Many of these bacteria scavenge iron by synthesizing and exporting small molecule siderophores that chelate iron. Iron-bound siderophores are subsequently imported for metabolic processing. Three related serine hydrolases have been characterized biochemically in this pathway: Fes, IroD, and IroE. Here, we report the crystal structure of IroE from uropathogenic Escherichia coli CFT073. The native structure and a complex with diisopropyl fluorophosphonate (DFP, a potent serine hydrolase inhibitor) were determined at 2.3 and 1.4 A resolution, respectively. IroE has the typical alpha/beta-hydrolase fold with an atypical catalytic dyad composed of Ser 189 and His 287. Mutation of either residue was detrimental to catalysis. In addition, rather than the typical oxyanion hole composed of backbone amides, IroE employs the atypical guanidinium moiety of Arg 130. Asp 90 anchors Arg 130 in the active site, and mutation of either residue was likewise detrimental to catalysis. We also compare the structure of IroE to the structure of Fes from Shigella flexneri (PDB entry 2B20). Both enzymes have similar active sites, but Fes has an additional amino-terminal lid domain. These lid domains are proposed to confer specificity to these related hydrolases.
-==About this Structure==
+Structural characterization of enterobactin hydrolase IroE.,Larsen NA, Lin H, Wei R, Fischbach MA, Walsh CT Biochemistry. 2006 Aug 29;45(34):10184-90. PMID:16922493<ref>PMID:16922493</ref>
-GZR is a [http://en.wikipedia.org/wiki/Single_protein 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=2GZR OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Structural characterization of enterobactin hydrolase IroE., Larsen NA, Lin H, Wei R, Fischbach MA, Walsh CT, Biochemistry. 2006 Aug 29;45(34):10184-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16922493 16922493]
+</div>
+<div class="pdbe-citations 2gzr" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Larsen, N.A.]]
+[[Category: Larsen NA]]
-[[Category: Walsh, C.T.]]
+[[Category: Walsh CT]]
-[[Category: catalytic dyad]]
-[[Category: enterobactin]]
-[[Category: serine hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:11:12 2008''