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==Structure of Lactococcus lactis ZitR, wild type in complex with DNA== | ==Structure of Lactococcus lactis ZitR, wild type in complex with DNA== | ||
<StructureSection load='5yi2' size='340' side='right' caption='[[5yi2]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='5yi2' size='340' side='right'caption='[[5yi2]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5yi2]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YI2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5yi2]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Lacla Lacla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YI2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5yhy|5yhy]], [[5yhx|5yhx]], [[5yhz|5yhz]], [[5yi1|5yi1]], [[5yi0|5yi0]], [[5yi3|5yi3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5yhy|5yhy]], [[5yhx|5yhx]], [[5yhz|5yhz]], [[5yi1|5yi1]], [[5yi0|5yi0]], [[5yi3|5yi3]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">zitR, L168265 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272623 LACLA])</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=5yi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yi2 OCA], [http://pdbe.org/5yi2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yi2 RCSB], [http://www.ebi.ac.uk/pdbsum/5yi2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yi2 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=5yi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yi2 OCA], [http://pdbe.org/5yi2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yi2 RCSB], [http://www.ebi.ac.uk/pdbsum/5yi2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yi2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Metalloregulators allosterically control transcriptional activity through metal binding-induced reorganization of ligand residues and/or hydrogen bonding networks, while the coordination atoms on the same ligand residues remain seldom changed. Here we show that the MarR-type zinc transcriptional regulator ZitR switches one of its histidine nitrogen atoms for zinc coordination during the allosteric control of DNA binding. The Zn(II)-coordination nitrogen on histidine 42 within ZitR's high-affinity zinc site (site 1) switches from Nepsilon2 to Ndelta1 upon Zn(II) binding to its low-affinity zinc site (site 2), which facilitates ZitR's conversion from the nonoptimal to the optimal DNA-binding conformation. This histidine switch-mediated cooperation between site 1 and site 2 enables ZitR to adjust its DNA-binding affinity in response to a broad range of zinc fluctuation, which may allow the fine tuning of transcriptional regulation. | |||
Allosteric histidine switch for regulation of intracellular zinc(II) fluctuation.,Zhu R, Song Y, Liu H, Yang Y, Wang S, Yi C, Chen PR Proc Natl Acad Sci U S A. 2017 Dec 26;114(52):13661-13666. doi:, 10.1073/pnas.1708563115. Epub 2017 Dec 11. PMID:29229866<ref>PMID:29229866</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5yi2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Lacla]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen, P]] | [[Category: Chen, P]] | ||
[[Category: Liu, H]] | [[Category: Liu, H]] | ||
Revision as of 15:43, 25 December 2019
Structure of Lactococcus lactis ZitR, wild type in complex with DNAStructure of Lactococcus lactis ZitR, wild type in complex with DNA
Structural highlights
Publication Abstract from PubMedMetalloregulators allosterically control transcriptional activity through metal binding-induced reorganization of ligand residues and/or hydrogen bonding networks, while the coordination atoms on the same ligand residues remain seldom changed. Here we show that the MarR-type zinc transcriptional regulator ZitR switches one of its histidine nitrogen atoms for zinc coordination during the allosteric control of DNA binding. The Zn(II)-coordination nitrogen on histidine 42 within ZitR's high-affinity zinc site (site 1) switches from Nepsilon2 to Ndelta1 upon Zn(II) binding to its low-affinity zinc site (site 2), which facilitates ZitR's conversion from the nonoptimal to the optimal DNA-binding conformation. This histidine switch-mediated cooperation between site 1 and site 2 enables ZitR to adjust its DNA-binding affinity in response to a broad range of zinc fluctuation, which may allow the fine tuning of transcriptional regulation. Allosteric histidine switch for regulation of intracellular zinc(II) fluctuation.,Zhu R, Song Y, Liu H, Yang Y, Wang S, Yi C, Chen PR Proc Natl Acad Sci U S A. 2017 Dec 26;114(52):13661-13666. doi:, 10.1073/pnas.1708563115. Epub 2017 Dec 11. PMID:29229866[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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