3f2g: Difference between revisions

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-[[Image:3f2g.png|left|200px]]
+==Crystal structure of MerB mutant C160S, the Organomercurial Lyase involved in a bacterial mercury resistance system==
+<StructureSection load='3f2g' size='340' side='right' caption='[[3f2g]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3f2g]] is a 2 chain structure with 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=3F2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F2G FirstGlance]. <br>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1s6l|1s6l]], [[3f0o|3f0o]], [[3f0p|3f0p]], [[3f2f|3f2f]], [[3f2h|3f2h]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">merB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3f2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3f2g RCSB], [http://www.ebi.ac.uk/pdbsum/3f2g PDBsum]</span></td></tr>
+</table>
+== 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/f2/3f2g_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/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Bacteria resistant to methylmercury utilize two enzymes (MerA and MerB) to degrade methylmercury to the less toxic elemental mercury. The crucial step is the cleavage of the carbon-mercury bond of methylmercury by the organomercurial lyase (MerB). In this study, we determined high resolution crystal structures of MerB in both the free (1.76-A resolution) and mercury-bound (1.64-A resolution) states. The crystal structure of free MerB is very similar to the NMR structure, but important differences are observed when comparing the two structures. In the crystal structure, an amino-terminal alpha-helix that is not present in the NMR structure makes contact with the core region adjacent to the catalytic site. This interaction between the amino-terminal helix and the core serves to bury the active site of MerB. The crystal structures also provide detailed insights into the mechanism of carbon-mercury bond cleavage by MerB. The structures demonstrate that two conserved cysteines (Cys-96 and Cys-159) play a role in substrate binding, carbon-mercury bond cleavage, and controlled product (ionic mercury) release. In addition, the structures establish that an aspartic acid (Asp-99) in the active site plays a crucial role in the proton transfer step required for the cleavage of the carbon-mercury bond. These findings are an important step in understanding the mechanism of carbon-mercury bond cleavage by MerB.
-{{STRUCTURE_3f2g|  PDB=3f2g  |  SCENE=  }}
+Crystal structures of the organomercurial lyase MerB in its free and mercury-bound forms: insights into the mechanism of methylmercury degradation.,Lafrance-Vanasse J, Lefebvre M, Di Lello P, Sygusch J, Omichinski JG J Biol Chem. 2009 Jan 9;284(2):938-44. Epub 2008 Nov 12. PMID:19004822<ref>PMID:19004822</ref>
-===Crystal structure of MerB mutant C160S, the Organomercurial Lyase involved in a bacterial mercury resistance system===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_19004822}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[3f2g]] is a 2 chain structure with 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=3F2G OCA].
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:019004822</ref><references group="xtra"/>
 [[Category: Alkylmercury lyase]]
 [[Category: Escherichia coli]]
-[[Category: Lafrance-Vanasse, J.]]
+[[Category: Lafrance-Vanasse, J]]
-[[Category: Lefebvre, M.]]
+[[Category: Lefebvre, M]]
-[[Category: Lello, P Di.]]
+[[Category: Lello, P Di]]
-[[Category: Omichinski, J G.]]
+[[Category: Omichinski, J G]]
-[[Category: Sygusch, J.]]
+[[Category: Sygusch, J]]
-[[Category: Alkylmercury lyase]]
 [[Category: Lyase]]
 [[Category: Merb]]