3f2g: Difference between revisions

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-{{Seed}}
-[[Image:3f2g.png|left|200px]]
-<!--
+==Crystal structure of MerB mutant C160S, the Organomercurial Lyase involved in a bacterial mercury resistance system==
-The line below this paragraph, containing "STRUCTURE_3f2g", creates the "Structure Box" on the page.
+<StructureSection load='3f2g' size='340' side='right'caption='[[3f2g]], [[Resolution|resolution]] 1.78&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'>[[3f2g]] 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=3F2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F2G 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]] 1.781&#8491;</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=3f2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f2g OCA], [https://pdbe.org/3f2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f2g RCSB], [https://www.ebi.ac.uk/pdbsum/3f2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f2g ProSAT]</span></td></tr>
-{{STRUCTURE_3f2g|  PDB=3f2g  |  SCENE=  }}
+</table>
+== Function ==
+[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/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/main_output.php?pdb_ID=3f2g 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.
-===Crystal structure of MerB mutant C160S, the Organomercurial Lyase involved in a bacterial mercury resistance system===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_19004822}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3f2g" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 19004822 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19004822}}
+__TOC__
+</StructureSection>
-==About this Structure==
-F2G 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=3F2G OCA].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/19004822 19004822]
-[[Category: Alkylmercury lyase]]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
+[[Category: Di Lello P]]
-[[Category: Alkylmercury lyase]]
+[[Category: Lafrance-Vanasse J]]
-[[Category: Merb]]
+[[Category: Lefebvre M]]
-[[Category: Mercuric resistance]]
+[[Category: Omichinski JG]]
-[[Category: Mercury resistance]]
+[[Category: Sygusch J]]
-[[Category: Organomercurial lyase]]
-[[Category: Plasmid]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 21 20:46:09 2009''