1ON2

Bacillus subtilis Manganese Transport Regulator (MntR), D8M Mutant, Bound to Manganese

Summary for 1ON2

• Entry DOI: 10.2210/pdb1on2/pdb
• Related: 1ON1
• Descriptor: Transcriptional regulator mntR, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: helix-turn-helix, dna-binding protein, metalloregulatory protein, transcription
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm (Probable): P54512
• Total number of polymer chains: 2
• Total formula weight: 33716.36

Authors

Glasfeld, A.,Guedon, E.,Helmann, J.D.,Brennan, R.G. (deposition date: 2003-02-26, release date: 2003-07-15, Last modification date: 2024-02-14)

Primary citation

Glasfeld, A.,Guedon, E.,Helmann, J.D.,Brennan, R.G.
Structure of the Manganese-Bound Manganese Transport Regulator of Bacillus subtilis
Nat.Struct.Biol., 10:652-657, 2003

PubMed Abstract: The Bacillus subtilis manganese transport regulator, MntR, binds Mn2+ as an effector and is a repressor of transporters that import manganese. A member of the diphtheria toxin repressor (DtxR) family of metalloregulatory proteins, MntR exhibits selectivity for Mn2+ over Fe2+. Replacement of a metal-binding residue, Asp8, with methionine (D8M) relaxes this specificity. We report here the X-ray crystal structures of wild-type MntR and the D8M mutant bound to manganese with 1.75 A and 1.61 A resolution, respectively. The 142-residue MntR homodimer has substantial structural similarity to the 226-residue DtxR but lacks the C-terminal SH3-like domain of DtxR. The metal-binding pockets of MntR and DtxR are substantially different. The cation-to-cation distance between the two manganese ions bound by MntR is 3.3 A, whereas that between the metal ions bound by DtxR is 9 A. D8M binds only a single Mn2+ per monomer, owing to alteration of the metal-binding site. The sole retained metal site adopts pseudo-hexacoordinate geometry rather than the pseudo-heptacoordinate geometry of the MntR metal sites.

PubMed: 12847518
DOI: 10.1038/nsb951

Experimental method

X-RAY DIFFRACTION (1.61 Å)