2JJ7

Crystal structure of the HlyIIR mutant protein with residues 170-185 substituted by alanine

Summary for 2JJ7

• Entry DOI: 10.2210/pdb2jj7/pdb
• Related: 2FX0
• Descriptor: HEMOLYSIN II REGULATORY PROTEIN (2 entities in total)
• Functional Keywords: dna-binding protein, transcription regulation, dna-binding, tetr family, transcription, transcriptional regulator
• Biological source: BACILLUS CEREUS
• Total number of polymer chains: 2
• Total formula weight: 43221.59

Authors

Kovalevskiy, O.V.,Antson, A.A.,Solonin, A.S. (deposition date: 2008-03-18, release date: 2008-04-08, Last modification date: 2023-12-13)

Primary citation

Kovalevskii, O.V.,Antson, A.A.,Solonin, A.S.
[Contraction of the disordered loop located within C-terminal domain of the transcriptional regulator HlyIIR causes its structural rearrangement].
Mol.Biol.(Moscow), 43:126-135, 2009

PubMed Abstract: HlyIIR is a negative transcriptional regulator of the hemolysin II gene from . A disordered region (amino acid residues 170-185) localized within the C-terminal domain near the dimerization interface was found in the recently determined HlyIIR X-ray structure. To clarify the effect of this region on HlyIIR properties and potential improvement of the diffraction quality of its crystals, we constructed a HlyIIR mutant with a single alanine residue substituting for the overall disordered region. According to biochemical analysis, the mutant protein still formed a dimer but lost its DNA-binding activity. Its crystals displayed better diffraction quality as compared with the native protein. The mutant structure was determined by X-ray analysis with a resolution of 2.1 Å. However, the mutant protein formed an alternative dimer differing from the wild-type dimer, as its subunits were rotated by 160. The conformation of individual subunits also partially changed. As this considerable remodeling in the mutant protein structure resulted from the conformational changes in the segment Pro161-Ser169, we concluded that this segment was important for maintaining the native HlyIIR structure.

PubMed: 19334535

Experimental method

X-RAY DIFFRACTION (2.1 Å)