5YI2

Structure of Lactococcus lactis ZitR, wild type in complex with DNA

Summary for 5YI2

• Entry DOI: 10.2210/pdb5yi2/pdb
• Related: 5YHX 5YHY 5YHZ 5YI0 5YI1 5YI3
• Descriptor: Zinc transport transcriptional regulator, DNA (5'-D(*TP*GP*TP*TP*AP*AP*CP*TP*AP*GP*TP*TP*AP*AP*CP*A)-3'), ZINC ION, ... (4 entities in total)
• Functional Keywords: zinc binding protein, marr family, winged helix-turn-helix, transcriptional regulator, metal binding protein
• Biological source: Lactococcus lactis subsp. lactis (Streptococcus lactis); More
• Total number of polymer chains: 16
• Total formula weight: 171782.26

Authors

Song, Y.,Liu, H.,Zhu, R.,Yi, C.,Chen, P. (deposition date: 2017-10-01, release date: 2017-12-06, Last modification date: 2023-11-22)

Primary citation

Zhu, R.,Song, Y.,Liu, H.,Yang, Y.,Wang, S.,Yi, C.,Chen, P.R.
Allosteric histidine switch for regulation of intracellular zinc(II) fluctuation.
Proc.Natl.Acad.Sci.USA, 114:13661-13666, 2017

PubMed Abstract: 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 Nε2 to Nδ1 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.

PubMed: 29229866
DOI: 10.1073/pnas.1708563115

Experimental method

X-RAY DIFFRACTION (2.6 Å)