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The crystal structure of the transcriptional regulator HucR from Deinococcus radiodurans reveals a repressor preconfigured for DNA binding.
J Mol Biol. 2006 Jun 30; 360(1):168-77.JM

Abstract

We report here the 2.3 A resolution structure of the hypothetical uricase regulator (HucR) from Deinococcus radiodurans R1. HucR, a member of the MarR family of DNA-binding proteins, was previously shown to repress its own expression as well as that of a uricase, a repression that is alleviated both in vivo and in vitro upon binding uric acid, the substrate for uricase. As uric acid is a potent scavenger of reactive oxygen species, and as D. radiodurans is known for its remarkable resistance to DNA-damaging agents, these observations indicate a novel oxidative stress response mechanism. The crystal structure of HucR in the absence of ligand or DNA reveals a dimer in which the DNA recognition helices are preconfigured for DNA binding. This configuration of DNA-binding domains is achieved through an apparently stable dimer interface that, in contrast to what is observed in other MarR homologs for which structures have been determined, shows little conformational heterogeneity in the absence of ligand. An additional amino-terminal segment, absent from other MarR homologs, appears to brace the principal helix of the dimerization interface. However, although HucR is preconfigured for DNA binding, the presence of a stacked pair of symmetry-related histidine residues at a central pivot point in the dimer interface suggests a mechanism for a conformational change to attenuate DNA binding.

Authors+Show Affiliations

Bordelon T
Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.
Wilkinson SP
No affiliation info available
Grove A
No affiliation info available
Newcomer ME
No affiliation info available

MeSH

Amino Acid SequenceBacterial ProteinsCrystallography, X-RayDNADeinococcusGene Expression Regulation, BacterialHydrogen-Ion ConcentrationModels, MolecularMolecular Sequence DataProtein BindingProtein ConformationRepressor ProteinsSequence Homology, Amino AcidTranscription FactorsTranscription, Genetic

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16750221

Citation

Bordelon, Tee, et al. "The Crystal Structure of the Transcriptional Regulator HucR From Deinococcus Radiodurans Reveals a Repressor Preconfigured for DNA Binding." Journal of Molecular Biology, vol. 360, no. 1, 2006, pp. 168-77.
Bordelon T, Wilkinson SP, Grove A, et al. The crystal structure of the transcriptional regulator HucR from Deinococcus radiodurans reveals a repressor preconfigured for DNA binding. J Mol Biol. 2006;360(1):168-77.
Bordelon, T., Wilkinson, S. P., Grove, A., & Newcomer, M. E. (2006). The crystal structure of the transcriptional regulator HucR from Deinococcus radiodurans reveals a repressor preconfigured for DNA binding. Journal of Molecular Biology, 360(1), 168-77.
Bordelon T, et al. The Crystal Structure of the Transcriptional Regulator HucR From Deinococcus Radiodurans Reveals a Repressor Preconfigured for DNA Binding. J Mol Biol. 2006 Jun 30;360(1):168-77. PubMed PMID: 16750221.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The crystal structure of the transcriptional regulator HucR from Deinococcus radiodurans reveals a repressor preconfigured for DNA binding. AU - Bordelon,Tee, AU - Wilkinson,Steven P, AU - Grove,Anne, AU - Newcomer,Marcia E, Y1 - 2006/05/19/ PY - 2006/03/17/received PY - 2006/04/28/revised PY - 2006/05/02/accepted PY - 2006/6/6/pubmed PY - 2006/8/15/medline PY - 2006/6/6/entrez SP - 168 EP - 77 JF - Journal of molecular biology JO - J Mol Biol VL - 360 IS - 1 N2 - We report here the 2.3 A resolution structure of the hypothetical uricase regulator (HucR) from Deinococcus radiodurans R1. HucR, a member of the MarR family of DNA-binding proteins, was previously shown to repress its own expression as well as that of a uricase, a repression that is alleviated both in vivo and in vitro upon binding uric acid, the substrate for uricase. As uric acid is a potent scavenger of reactive oxygen species, and as D. radiodurans is known for its remarkable resistance to DNA-damaging agents, these observations indicate a novel oxidative stress response mechanism. The crystal structure of HucR in the absence of ligand or DNA reveals a dimer in which the DNA recognition helices are preconfigured for DNA binding. This configuration of DNA-binding domains is achieved through an apparently stable dimer interface that, in contrast to what is observed in other MarR homologs for which structures have been determined, shows little conformational heterogeneity in the absence of ligand. An additional amino-terminal segment, absent from other MarR homologs, appears to brace the principal helix of the dimerization interface. However, although HucR is preconfigured for DNA binding, the presence of a stacked pair of symmetry-related histidine residues at a central pivot point in the dimer interface suggests a mechanism for a conformational change to attenuate DNA binding. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/16750221/The_crystal_structure_of_the_transcriptional_regulator_HucR_from_Deinococcus_radiodurans_reveals_a_repressor_preconfigured_for_DNA_binding_ DB - PRIME DP - Unbound Medicine ER -