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7B0C

[4Fe-4S]-NsrR complexed to 23-bp HmpA1 operator fragment

Summary for 7B0C
Entry DOI10.2210/pdb7b0c/pdb
DescriptorHTH-type transcriptional repressor NsrR, DNA (5'-D(P*AP*AP*CP*AP*CP*GP*AP*AP*TP*AP*TP*CP*AP*TP*CP*TP*AP*CP*CP*AP*AP*TP*T)-3'), DNA (5'-D(P*AP*AP*TP*TP*GP*GP*TP*AP*GP*AP*TP*GP*AP*TP*AP*TP*TP*CP*GP*TP*GP*TP*T)-3'), ... (5 entities in total)
Functional Keywordsno sensor, iron sulfur cluster, transcription, dna complex, dna binding protein
Biological sourceStreptomyces coelicolor A3(2)
More
Total number of polymer chains4
Total formula weight49826.68
Authors
Rohac, R.,Fontecilla-Camps, J.C.,Volbeda, A. (deposition date: 2020-11-19, release date: 2022-06-01, Last modification date: 2024-01-31)
Primary citationRohac, R.,Crack, J.C.,de Rosny, E.,Gigarel, O.,Le Brun, N.E.,Fontecilla-Camps, J.C.,Volbeda, A.
Structural determinants of DNA recognition by the NO sensor NsrR and related Rrf2-type [FeS]-transcription factors.
Commun Biol, 5:769-769, 2022
Cited by
PubMed Abstract: Several transcription factors of the Rrf2 family use an iron-sulfur cluster to regulate DNA binding through effectors such as nitric oxide (NO), cellular redox status and iron levels. [4Fe-4S]-NsrR from Streptomyces coelicolor (ScNsrR) modulates expression of three different genes via reaction and complex formation with variable amounts of NO, which results in detoxification of this gas. Here, we report the crystal structure of ScNsrR complexed with an hmpA1 gene operator fragment and compare it with those previously reported for [2Fe-2S]-RsrR/rsrR and apo-IscR/hyA complexes. Important structural differences reside in the variation of the DNA minor and major groove widths. In addition, different DNA curvatures and different interactions with the protein sensors are observed. We also report studies of NsrR binding to four hmpA1 variants, which indicate that flexibility in the central region is not a key binding determinant. Our study explores the promotor binding specificities of three closely related transcriptional regulators.
PubMed: 35908109
DOI: 10.1038/s42003-022-03745-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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