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| | <StructureSection load='5crl' size='340' side='right'caption='[[5crl]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='5crl' size='340' side='right'caption='[[5crl]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5crl]] is a 2 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=5CRL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CRL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5crl]] is a 2 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=5CRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CRL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">merR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=5crl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5crl OCA], [https://pdbe.org/5crl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5crl RCSB], [https://www.ebi.ac.uk/pdbsum/5crl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5crl ProSAT]</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=5crl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5crl OCA], [http://pdbe.org/5crl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5crl RCSB], [http://www.ebi.ac.uk/pdbsum/5crl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5crl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MERR_PSEAI MERR_PSEAI]] Mediates the mercuric-dependent induction of mercury resistance operon. In the absence of mercury MerR represses transcription by binding tightly to the mer operator region; when mercury is present the dimeric complex binds a single ion and becomes a potent transcriptional activator, while remaining bound to the mer site. | + | [https://www.uniprot.org/uniprot/MERR_PSEAI MERR_PSEAI] Mediates the mercuric-dependent induction of mercury resistance operon. In the absence of mercury MerR represses transcription by binding tightly to the mer operator region; when mercury is present the dimeric complex binds a single ion and becomes a potent transcriptional activator, while remaining bound to the mer site. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5crl" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5crl" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, H]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Gan, J H]] | + | [[Category: Chen H]] |
| - | [[Category: Wang, D]] | + | [[Category: Gan JH]] |
| - | [[Category: Mercury]] | + | [[Category: Wang D]] |
| - | [[Category: Merr]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: P. aeruginosa tn501]]
| + | |
| - | [[Category: Transcription activator]]
| + | |
| Structural highlights
Function
MERR_PSEAI Mediates the mercuric-dependent induction of mercury resistance operon. In the absence of mercury MerR represses transcription by binding tightly to the mer operator region; when mercury is present the dimeric complex binds a single ion and becomes a potent transcriptional activator, while remaining bound to the mer site.
Publication Abstract from PubMed
The metalloprotein MerR is a mercury(II)-dependent transcriptional repressor-activator that responds to mercury(II) with extraordinary sensitivity and selectivity. It's widely distributed in both Gram-negative and Gram-positive bacteria but with barely detectable sequence identities between the two sources. To provide structural basis for the considerable biochemical and biophysical experiments previously performed on Tn501 and Tn21 MerR from Gram-negative bacteria, we analyzed the crystal structure of mercury(II)-bound Tn501 MerR. The structure in the metal-binding domain provides Tn501 MerR with a high affinity for mercury(II) and the ability to distinguish mercury(II) from other metals with its unique planar trigonal coordination geometry, which is adopted by both Gram-negative and Gram-positive bacteria. The mercury(II) coordination state in the C-terminal metal-binding domain is transmitted through the allosteric network across the dimer interface to the N-terminal DNA-binding domain. Together with the previous mutagenesis analyses, the present data indicate that the residues in the allosteric pathway have a central role in maintaining the functions of Tn501 MerR. In addition, the complex structure exhibits significant differences in tertiary and quaternary structural arrangements compared to those of Bacillus MerR from Gram-positive bacteria, which probably enable them to function with specific promoter DNA with different spacers between -35 and -10 elements.
Structural Analysis of the Hg(II)-Regulatory Protein Tn501 MerR from Pseudomonas aeruginosa.,Wang D, Huang S, Liu P, Liu X, He Y, Chen W, Hu Q, Wei T, Gan J, Ma J, Chen H Sci Rep. 2016 Sep 19;6:33391. doi: 10.1038/srep33391. PMID:27641146[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wang D, Huang S, Liu P, Liu X, He Y, Chen W, Hu Q, Wei T, Gan J, Ma J, Chen H. Structural Analysis of the Hg(II)-Regulatory Protein Tn501 MerR from Pseudomonas aeruginosa. Sci Rep. 2016 Sep 19;6:33391. doi: 10.1038/srep33391. PMID:27641146 doi:http://dx.doi.org/10.1038/srep33391
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