1s6l: Difference between revisions

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-[[Image:1s6l.gif|left|200px]]<br /><applet load="1s6l" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1s6l" />
-'''Solution structure of MerB, the Organomercurial Lyase involved in the bacterial mercury resistance system'''<br />
-==Overview==
+==Solution structure of MerB, the Organomercurial Lyase involved in the bacterial mercury resistance system==
-Mercury resistant bacteria have developed a system of two enzymes (MerA and MerB), which allows them to efficiently detoxify both ionic and organomercurial compounds. The organomercurial lyase (MerB) catalyzes the protonolysis of the carbon-mercury bond resulting in the formation of ionic mercury and a reduced hydrocarbon. The ionic mercury [Hg(II)] is subsequently reduced to the less reactive elemental mercury [Hg(0)] by a specific mercuric reductase (MerA). To better understand MerB's unique enzymatic activity, we used nuclear magnetic resonance (NMR) spectroscopy to determine the structure of the free enzyme. MerB is characterized by a novel protein fold consisting of three noninteracting antiparallel beta-sheets surrounded by six alpha-helices. By comparing the NMR data of free MerB and the MerB/Hg/DTT complex, we identified a set of residues that likely define a Hg/DTT binding site. These residues cluster around two cysteines (C(96) and C(159)) that are crucial to MerB's catalytic activity. A detailed analysis of the structure revealed the presence of an extensive hydrophobic groove adjacent to this Hg/DTT binding site. This extensive hydrophobic groove has the potential to interact with the hydrocarbon moiety of a wide variety of substrates and may explain the broad substrate specificity of MerB.
+<StructureSection load='1s6l' size='340' side='right'caption='[[1s6l]]' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[1s6l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S6L FirstGlance]. <br>
-S6L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Alkylmercury_lyase Alkylmercury lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.2 4.99.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S6L OCA].
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1s6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s6l OCA], [https://pdbe.org/1s6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s6l RCSB], [https://www.ebi.ac.uk/pdbsum/1s6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s6l ProSAT]</span></td></tr>
-==Reference==
+</table>
-NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyase involved in the bacterial mercury resistance system., Di Lello P, Benison GC, Valafar H, Pitts KE, Summers AO, Legault P, Omichinski JG, Biochemistry. 2004 Jul 6;43(26):8322-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15222745 15222745]
+== Function ==
-[[Category: Alkylmercury lyase]]
+[https://www.uniprot.org/uniprot/MERB_ECOLX MERB_ECOLX] Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg(2+), which is subsequently detoxified by the mercuric reductase (By similarity).
+== 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/s6/1s6l_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=1s6l ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Benison, G C.]]
+[[Category: Benison GC]]
-[[Category: Legault, P.]]
+[[Category: Di Lello P]]
-[[Category: Lello, P Di.]]
+[[Category: Legault P]]
-[[Category: Omichinski, J G.]]
+[[Category: Omichinski JG]]
-[[Category: Pitts, K E.]]
+[[Category: Pitts KE]]
-[[Category: Summers, A O.]]
+[[Category: Summers AO]]
-[[Category: Valafar, H.]]
+[[Category: Valafar H]]
-[[Category: lyase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:30 2008''