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| | <StructureSection load='1r1v' size='340' side='right'caption='[[1r1v]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1r1v' size='340' side='right'caption='[[1r1v]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1r1v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1V OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R1V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1r1v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R1V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1r1u|1r1u]], [[1r1t|1r1t]], [[1smt|1smt]], [[1r22|1r22]], [[1r23|1r23]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">czrA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 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=1r1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1v OCA], [https://pdbe.org/1r1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r1v RCSB], [https://www.ebi.ac.uk/pdbsum/1r1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r1v ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1v OCA], [http://pdbe.org/1r1v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r1v RCSB], [http://www.ebi.ac.uk/pdbsum/1r1v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r1v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O85142_STAAU O85142_STAAU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1r1v" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1r1v" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[CzrA 3D structures|CzrA 3D structures]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, X]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Eicken, C]] | + | [[Category: Chen X]] |
| - | [[Category: Giedroc, D P]] | + | [[Category: Eicken C]] |
| - | [[Category: Koshlap, K M]] | + | [[Category: Giedroc DP]] |
| - | [[Category: Pennella, M A]] | + | [[Category: Koshlap KM]] |
| - | [[Category: Sacchettini, J C]] | + | [[Category: Pennella MA]] |
| - | [[Category: VanZile, M L]] | + | [[Category: Sacchettini JC]] |
| - | [[Category: Dna binding]]
| + | [[Category: VanZile ML]] |
| - | [[Category: Transcription repressor]]
| + | |
| - | [[Category: Transcriptional regulation]]
| + | |
| - | [[Category: Winged hth protein]]
| + | |
| Structural highlights
Function
O85142_STAAU
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
The origin of metal ion selectivity by members of the SmtB/ArsR family of bacterial metal-sensing transcriptional repressors and the mechanism of negative allosteric regulation of DNA binding is poorly understood. Here, we report that two homologous zinc sensors, Staphylococcus aureus CzrA and cyanobacterial SmtB, are "winged" helix homodimeric DNA-binding proteins that bind Zn(II) to a pair of tetrahedral, interhelical binding sites, with two ligands derived from the alpha5 helix of one subunit, Asp84 O(delta1) (Asp104 in SmtB), His86 N(delta1) (His106), and two derived from the alpha5 helix of the other, His97' N(delta1) (His117') and His100' N(epsilon2) (Glu120'). Formation of the metal chelate drives a quaternary structural switch mediated by an intersubunit hydrogen-binding network that originates with the non-liganding N(epsilon2) face of His97 in CzrA (His117 in SmtB) that stabilizes a low-affinity, DNA-binding conformation. The structure of the Zn(1) SmtB homodimer shows that both metal-binding sites of the dimer must be occupied for the quaternary structural switch to occur. Thus, a critical zinc-ligating histidine residue obligatorily couples formation of the metal-sensing coordination chelate to changes in the conformation and dynamics of the putative DNA-binding helices.
A metal-ligand-mediated intersubunit allosteric switch in related SmtB/ArsR zinc sensor proteins.,Eicken C, Pennella MA, Chen X, Koshlap KM, VanZile ML, Sacchettini JC, Giedroc DP J Mol Biol. 2003 Oct 31;333(4):683-95. PMID:14568530[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Eicken C, Pennella MA, Chen X, Koshlap KM, VanZile ML, Sacchettini JC, Giedroc DP. A metal-ligand-mediated intersubunit allosteric switch in related SmtB/ArsR zinc sensor proteins. J Mol Biol. 2003 Oct 31;333(4):683-95. PMID:14568530
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