View source for 5fmn


==The nickel-responsive transcriptional regulator InrS==
<StructureSection load='5fmn' size='340' side='right'caption='[[5fmn]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fmn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FMN 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]] 2.4&#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=5fmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fmn OCA], [https://pdbe.org/5fmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fmn RCSB], [https://www.ebi.ac.uk/pdbsum/5fmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fmn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q55554_SYNY3 Q55554_SYNY3] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The metal affinities of metal-sensing transcriptional regulators co-vary with cellular metal concentrations over more than 12 orders of magnitude. To understand the cause of this relationship, we determined the structure of the Ni(II) sensor InrS and then created cyanobacteria (Synechocystis PCC 6803) in which transcription of genes encoding a Ni(II) exporter and a Ni(II) importer were controlled by InrS variants with weaker Ni(II) affinities. Variant strains were sensitive to elevated nickel and contained more nickel, but the increase was small compared with the change in Ni(II) affinity. All of the variant sensors retained the allosteric mechanism that inhibits DNA binding following metal binding, but a response to nickel in vivo was observed only when the sensitivity was set to respond in a relatively narrow (less than two orders of magnitude) range of nickel concentrations. Thus, the Ni(II) affinity of InrS is attuned to cellular metal concentrations rather than the converse.

A tight tunable range for Ni(II) sensing and buffering in cells.,Foster AW, Pernil R, Patterson CJ, Scott AJ, Palsson LO, Pal R, Cummins I, Chivers PT, Pohl E, Robinson NJ Nat Chem Biol. 2017 Feb 6. doi: 10.1038/nchembio.2310. PMID:28166209<ref>PMID:28166209</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fmn" style="background-color:#fffaf0;"></div>

==See Also==
*[[Response regulator 3D structure|Response regulator 3D structure]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synechocystis sp. PCC 6803]]
[[Category: Foster AW]]
[[Category: Patterson CJ]]
[[Category: Pohl E]]
[[Category: Robinson NJ]]