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| | ==NMR structure of the cadmium metal-sensor CMTR from Mycobacterium tuberculosis== | | ==NMR structure of the cadmium metal-sensor CMTR from Mycobacterium tuberculosis== |
| - | <StructureSection load='2jsc' size='340' side='right'caption='[[2jsc]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='2jsc' size='340' side='right'caption='[[2jsc]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jsc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JSC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jsc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JSC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</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">Rv1994c, MT2050, MTCY39.25 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</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=2jsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jsc OCA], [https://pdbe.org/2jsc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jsc RCSB], [https://www.ebi.ac.uk/pdbsum/2jsc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jsc ProSAT]</span></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=2jsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jsc OCA], [https://pdbe.org/2jsc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jsc RCSB], [https://www.ebi.ac.uk/pdbsum/2jsc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jsc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CMTR_MYCTU CMTR_MYCTU] Metal-responsive transcriptional repressor for the cmt operon. Binding of cadmium or lead causes the repressor to dissociate from the DNA.<ref>PMID:12939264</ref> <ref>PMID:15966722</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Myctu]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Banci, L]] | + | [[Category: Banci L]] |
| - | [[Category: Bertini, I]] | + | [[Category: Bertini I]] |
| - | [[Category: Cantini, F]] | + | [[Category: Cantini F]] |
| - | [[Category: Cavet, J S]] | + | [[Category: Cavet JS]] |
| - | [[Category: Ciofi-Baffoni, S]] | + | [[Category: Ciofi-Baffoni S]] |
| - | [[Category: Dennison, C]] | + | [[Category: Dennison C]] |
| - | [[Category: Graham, A I]] | + | [[Category: Graham AI]] |
| - | [[Category: Harvie, D R]] | + | [[Category: Harvie DR]] |
| - | [[Category: Robinson, N J]] | + | [[Category: Robinson NJ]] |
| - | [[Category: SPINE, Structural Proteomics in Europe]]
| + | |
| - | [[Category: Cadmium]]
| + | |
| - | [[Category: Solution structure]]
| + | |
| - | [[Category: Spine]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structural proteomics in europe]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcriptional repressor]]
| + | |
| Structural highlights
Function
CMTR_MYCTU Metal-responsive transcriptional repressor for the cmt operon. Binding of cadmium or lead causes the repressor to dissociate from the DNA.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
CmtR from Mycobacterium tuberculosis is a winged helical DNA-binding repressor of the ArsR-SmtB metal-sensing family that senses cadmium and lead. Cadmium-CmtR is a dimer with the metal bound to Cys-102 from the C-terminal region of one subunit and two Cys associated with helix alphaR from the other subunit, forming a symmetrical pair of cadmium-binding sites. This is a significant novelty in the ArsR-SmtB family. The structure of the dimer could be solved at 312 K. The apoprotein at the same temperature is still a dimer, but it experiences a large conformational exchange at the dimer interface and within each monomer. This is monitored by an overall decrease of the number of nuclear Overhauser effects and by an increase of H(2)O-D(2)O exchange rates, especially at the dimeric interface, in the apo form with respect to the cadmium-bound state. The C-terminal tail region is completely unstructured in both apo and cadmium forms but becomes less mobile in the cadmium-bound protein due to the recruitment of Cys-102 as a metal-ligand. DNA binds to the apo dimer with a ratio 1:3 at millimolar concentration. Addition of cadmium to the apo-CmtR-DNA complex causes DNA detachment, restoring the NMR spectrum of free cadmium-CmtR. Cadmium binding across the dimer interface impairs DNA association by excluding the apo-conformers suited to bind DNA.
NMR structural analysis of cadmium sensing by winged helix repressor CmtR.,Banci L, Bertini I, Cantini F, Ciofi-Baffoni S, Cavet JS, Dennison C, Graham AI, Harvie DR, Robinson NJ J Biol Chem. 2007 Oct 12;282(41):30181-8. Epub 2007 Jun 27. PMID:17599915[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cavet JS, Graham AI, Meng W, Robinson NJ. A cadmium-lead-sensing ArsR-SmtB repressor with novel sensory sites. Complementary metal discrimination by NmtR AND CmtR in a common cytosol. J Biol Chem. 2003 Nov 7;278(45):44560-6. PMID:12939264 doi:10.1074/jbc.M307877200
- ↑ Wang Y, Hemmingsen L, Giedroc DP. Structural and functional characterization of Mycobacterium tuberculosis CmtR, a PbII/CdII-sensing SmtB/ArsR metalloregulatory repressor. Biochemistry. 2005 Jun 28;44(25):8976-88. PMID:15966722 doi:10.1021/bi050094v
- ↑ Banci L, Bertini I, Cantini F, Ciofi-Baffoni S, Cavet JS, Dennison C, Graham AI, Harvie DR, Robinson NJ. NMR structural analysis of cadmium sensing by winged helix repressor CmtR. J Biol Chem. 2007 Oct 12;282(41):30181-8. Epub 2007 Jun 27. PMID:17599915 doi:10.1074/jbc.M701119200
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