1afj: Difference between revisions

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 ==STRUCTURE OF THE MERCURY-BOUND FORM OF MERP, THE PERIPLASMIC PROTEIN FROM THE BACTERIAL MERCURY DETOXIFICATION SYSTEM, NMR, 20 STRUCTURES==
-<StructureSection load='1afj' size='340' side='right'caption='[[1afj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1afj' size='340' side='right'caption='[[1afj]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1afj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AFJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1afj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AFJ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
+</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MERP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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=1afj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1afj OCA], [https://pdbe.org/1afj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1afj RCSB], [https://www.ebi.ac.uk/pdbsum/1afj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1afj ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/MERP_SHIFL MERP_SHIFL]] Mercury scavenger that specifically binds to one mercury ion and which passes it to the mercuric reductase (MerA) via the MerT protein.
+[https://www.uniprot.org/uniprot/MERP_SHIFL MERP_SHIFL] Mercury scavenger that specifically binds to one mercury ion and which passes it to the mercuric reductase (MerA) via the MerT protein.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1afj ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Bacteria carrying plasmids with the mer operon, which encodes the proteins responsible for the bacterial mercury detoxification system, have the ability to transport Hg(II) across the cell membrane into the cytoplasm where it is reduced to Hg(0). This is significant because metallic mercury is relatively nontoxic and volatile and thus can be passively eliminated. The structures of the reduced and mercury-bound forms of merP, the periplasmic protein, which binds Hg(II) and transfers it to the membrane transport protein merT, have been determined in aqueous solution by multidimensional NMR spectroscopy. The 72-residue merP protein has a betaalpha betabeta alphabeta fold with the two alpha helices overlaying a four-strand antiparallel beta sheet. Structural differences between the reduced and mercury-bound forms of merP are localized to the metal binding loop containing the consensus sequence GMTCXXC. The structure of the mercury-bound form of merP shows that Hg(II) is bicoordinate with the Cys side chain ligands, and this is confirmed by the chemical shift frequency of the 199Hg resonance.
-Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system.,Steele RA, Opella SJ Biochemistry. 1997 Jun 10;36(23):6885-95. PMID:9188683<ref>PMID:9188683</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1afj" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Shigella paradysenteriae weldin 1927]]
 [[Category: Large Structures]]
-[[Category: Opella, S J]]
+[[Category: Shigella flexneri]]
-[[Category: Steele, R A]]
+[[Category: Opella SJ]]
-[[Category: Alpha-beta sandwich]]
+[[Category: Steele RA]]
-[[Category: Heavy metal transport]]
-[[Category: Mercury detoxification]]
-[[Category: Periplasmic]]