1ON1
Bacillus Subtilis Manganese Transport Regulator (Mntr) Bound To Manganese, AB Conformation.
Summary for 1ON1
| Entry DOI | 10.2210/pdb1on1/pdb |
| Related | 1ON2 |
| 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 | 33794.02 |
| Authors | Glasfeld, A.,Guedon, E.,Helmann, J.D.,Brennan, R.G. (deposition date: 2003-02-26, release date: 2003-07-15, Last modification date: 2023-08-16) |
| 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 Cited by 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: 12847518DOI: 10.1038/nsb951 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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