The nickel-responsive transcriptional regulator InrSThe nickel-responsive transcriptional regulator InrS

Structural highlights

5fmn is a 2 chain structure with sequence from Synechocystis sp. PCC 6803. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q55554_SYNY3

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

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

5fmn, resolution 2.40Å

Drag the structure with the mouse to rotate

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

OCA