5yi1: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5yi1 is ON HOLD
+==Structure of Lactococcus lactis ZitR, C30AH42A mutant in apo form==
+<StructureSection load='5yi1' size='340' side='right'caption='[[5yi1]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5yi1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis_Il1403 Lactococcus lactis subsp. lactis Il1403]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YI1 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]] 2.2&#8491;</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=5yi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yi1 OCA], [https://pdbe.org/5yi1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yi1 RCSB], [https://www.ebi.ac.uk/pdbsum/5yi1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yi1 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9CDU5_LACLA Q9CDU5_LACLA]
+<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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5yi1" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Lactococcus lactis subsp. lactis Il1403]]
+[[Category: Large Structures]]
+[[Category: Chen P]]
+[[Category: Liu H]]
+[[Category: Song Y]]
+[[Category: Yi C]]
+[[Category: Zhu R]]