6KTA

Crystal structure of B. halodurans MntR in apo form

Summary for 6KTA

• Entry DOI: 10.2210/pdb6kta/pdb
• Descriptor: HTH-type transcriptional regulator MntR, GLYCEROL (3 entities in total)
• Functional Keywords: mntr, transcription factor, transcription
• Biological source: Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
• Total number of polymer chains: 2
• Total formula weight: 33135.56

Authors

Lee, J.Y.,Lee, M.Y. (deposition date: 2019-08-26, release date: 2019-12-04, Last modification date: 2024-03-27)

Primary citation

Lee, M.Y.,Lee, D.W.,Joo, H.K.,Jeong, K.H.,Lee, J.Y.
Structural analysis of the manganese transport regulator MntR from Bacillus halodurans in apo and manganese bound forms.
Plos One, 14:e0224689-e0224689, 2019

PubMed Abstract: The manganese transport regulator MntR is a metal-ion activated transcriptional repressor of manganese transporter genes to maintain manganese ion homeostasis. MntR, a member of the diphtheria toxin repressor (DtxR) family of metalloregulators, selectively responds to Mn2+ and Cd2+ over Fe2+, Co2+ and Zn2+. The DtxR/MntR family members are well conserved transcriptional repressors that regulate the expression of metal ion uptake genes by sensing the metal ion concentration. MntR functions as a homo-dimer with one metal ion binding site per subunit. Each MntR subunit contains two domains: an N-terminal DNA binding domain, and a C-terminal dimerization domain. However, it lacks the C-terminal SH3-like domain of DtxR/IdeR. The metal ion binding site of MntR is located at the interface of the two domains, whereas the DtxR/IdeR subunit contains two metal ion binding sites, the primary and ancillary sites, separated by 9 Å. In this paper, we reported the crystal structures of the apo and Mn2+-bound forms of MntR from Bacillus halodurans, and analyze the structural basis of the metal ion binding site. The crystal structure of the Mn2+-bound form is almost identical to the apo form of MntR. In the Mn2+-bound structure, one subunit contains a binuclear cluster of manganese ions, the A and C sites, but the other subunit forms a mononuclear complex. Structural data about MntR from B. halodurans supports the previous hypothesizes about manganese-specific activation mechanism of MntR homologues.

PubMed: 31738781
DOI: 10.1371/journal.pone.0224689

Experimental method

X-RAY DIFFRACTION (2.3 Å)