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4m1p
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the copper-sensing repressor CsoR with Cu(I) from Geobacillus thermodenitrificans NG80-2== | |
| + | <StructureSection load='4m1p' size='340' side='right'caption='[[4m1p]], [[Resolution|resolution]] 2.56Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4m1p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_thermodenitrificans_NG80-2 Geobacillus thermodenitrificans NG80-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M1P FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.564Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4m1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m1p OCA], [https://pdbe.org/4m1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m1p RCSB], [https://www.ebi.ac.uk/pdbsum/4m1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m1p ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A4INJ9_GEOTN A4INJ9_GEOTN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The copper-sensing operon repressor (CsoR) is representative of a major Cu(I)-sensing family of bacterial metalloregulatory proteins that has evolved to prevent cytoplasmic copper toxicity. It is unknown how Cu(I) binding to tetrameric CsoRs mediates transcriptional derepression of copper resistance genes. A phylogenetic analysis of 227 DUF156 protein members, including biochemically or structurally characterized CsoR/RcnR repressors, reveals that Geobacillus thermodenitrificans (Gt) CsoR characterized here is representative of CsoRs from pathogenic bacilli Listeria monocytogenes and Bacillus anthracis. The 2.56 A structure of Cu(I)-bound Gt CsoR reveals that Cu(I) binding induces a kink in the alpha2-helix between two conserved copper-ligating residues and folds an N-terminal tail (residues 12-19) over the Cu(I) binding site. NMR studies of Gt CsoR reveal that this tail is flexible in the apo-state with these dynamics quenched upon Cu(I) binding. Small angle x-ray scattering experiments on an N-terminally truncated Gt CsoR (Delta2-10) reveal that the Cu(I)-bound tetramer is hydrodynamically more compact than is the apo-state. The implications of these findings for the allosteric mechanisms of other CsoR/RcnR repressors are discussed. | ||
| - | + | Cu(I)-mediated allosteric switching in a copper-sensing operon repressor (CsoR).,Chang FM, Coyne HJ, Cubillas C, Vinuesa P, Fang X, Ma Z, Ma D, Helmann JD, Garcia-de los Santos A, Wang YX, Dann CE 3rd, Giedroc DP J Biol Chem. 2014 Jul 4;289(27):19204-17. doi: 10.1074/jbc.M114.556704. Epub 2014, May 15. PMID:24831014<ref>PMID:24831014</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4m1p" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Geobacillus thermodenitrificans NG80-2]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chang F]] | ||
| + | [[Category: Dann III CE]] | ||
| + | [[Category: Giedroc DP]] | ||
Current revision
Crystal structure of the copper-sensing repressor CsoR with Cu(I) from Geobacillus thermodenitrificans NG80-2
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