5YI0
Structure of Lactococcus lactis ZitR, C30AH42A mutant
Summary for 5YI0
| Entry DOI | 10.2210/pdb5yi0/pdb |
| Related | 5YHX 5YHY 5YHZ 5YI1 5YI2 5YI3 |
| Descriptor | Zinc transport transcriptional regulator, ZINC ION (3 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 (strain IL1403) (Streptococcus lactis) |
| Total number of polymer chains | 4 |
| Total formula weight | 65648.09 |
| Authors | |
| 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 Cited by 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: 29229866DOI: 10.1073/pnas.1708563115 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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