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4k8d

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==Crystal structure of the C558(464)A/C559(465)A double mutant of Tn501 MerA in complex with NADPH and Hg2+==
==Crystal structure of the C558(464)A/C559(465)A double mutant of Tn501 MerA in complex with NADPH and Hg2+==
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<StructureSection load='4k8d' size='340' side='right' caption='[[4k8d]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
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<StructureSection load='4k8d' size='340' side='right'caption='[[4k8d]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4k8d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K8D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K8D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4k8d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K8D FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4k7z|4k7z]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4k8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k8d OCA], [https://pdbe.org/4k8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k8d RCSB], [https://www.ebi.ac.uk/pdbsum/4k8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k8d ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">merA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mercury(II)_reductase Mercury(II) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.1.1 1.16.1.1] </span></td></tr>
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<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=4k8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k8d OCA], [http://pdbe.org/4k8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k8d RCSB], [http://www.ebi.ac.uk/pdbsum/4k8d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k8d ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MERA_PSEAI MERA_PSEAI]] Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0).
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[https://www.uniprot.org/uniprot/MERA_PSEAI MERA_PSEAI] Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0).
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Dong, A]]
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[[Category: Large Structures]]
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[[Category: Falkowski, M]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Malone, M]]
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[[Category: Dong A]]
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[[Category: Miller, S M]]
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[[Category: Falkowski M]]
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[[Category: Pai, E F]]
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[[Category: Malone M]]
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[[Category: Flavoenzyme]]
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[[Category: Miller SM]]
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[[Category: Mercuric ion complex]]
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[[Category: Pai EF]]
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[[Category: Mercuric ion reductase]]
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[[Category: Nadph complex]]
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[[Category: Oxidoreductase]]
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[[Category: Reduced form]]
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[[Category: Ternary complex]]
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Revision as of 11:44, 30 November 2022

Crystal structure of the C558(464)A/C559(465)A double mutant of Tn501 MerA in complex with NADPH and Hg2+

PDB ID 4k8d

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