5FMN
The nickel-responsive transcriptional regulator InrS
Summary for 5FMN
| Entry DOI | 10.2210/pdb5fmn/pdb |
| Descriptor | INRS (2 entities in total) |
| Functional Keywords | dna binding protein, transcriptional regulator, nickel-binding protein |
| Biological source | SYNECHOCYSTIS SP. PCC 6803 |
| Total number of polymer chains | 2 |
| Total formula weight | 24081.54 |
| Authors | Foster, A.W.,Patterson, C.J.,Robinson, N.J.,Pohl, E. (deposition date: 2015-11-06, release date: 2017-02-01, Last modification date: 2024-05-08) |
| Primary citation | Foster, A.W.,Pernil, R.,Patterson, C.J.,Scott, A.J.,Palsson, L.O.,Pal, R.,Cummins, I.,Chivers, P.T.,Pohl, E.,Robinson, N.J. A tight tunable range for Ni(II) sensing and buffering in cells. Nat. Chem. Biol., 13:409-414, 2017 Cited by PubMed Abstract: 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. PubMed: 28166209DOI: 10.1038/nchembio.2310 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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