5yi0
From Proteopedia
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==Structure of Lactococcus lactis ZitR, C30AH42A mutant== | ==Structure of Lactococcus lactis ZitR, C30AH42A mutant== | ||
| - | <StructureSection load='5yi0' size='340' side='right' caption='[[5yi0]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='5yi0' size='340' side='right'caption='[[5yi0]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5yi0]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YI0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YI0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yi0]] is a 4 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=5YI0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YI0 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]], [[5yi2|5yi2]], [[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]], [[5yi2|5yi2]], [[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=5yi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yi0 OCA], [http://pdbe.org/5yi0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yi0 RCSB], [http://www.ebi.ac.uk/pdbsum/5yi0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yi0 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=5yi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yi0 OCA], [http://pdbe.org/5yi0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yi0 RCSB], [http://www.ebi.ac.uk/pdbsum/5yi0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yi0 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5yi0" 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 12:42, 25 December 2019
Structure of Lactococcus lactis ZitR, C30AH42A mutant
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