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| {{STRUCTURE_1on2| PDB=1on2 | SCENE= }} | | {{STRUCTURE_1on2| PDB=1on2 | SCENE= }} |
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| '''Bacillus subtilis Manganese Transport Regulator (MntR), D8M Mutant, Bound to Manganese'''
| | ===Bacillus subtilis Manganese Transport Regulator (MntR), D8M Mutant, Bound to Manganese=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_12847518}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12847518 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12847518}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Helix-turn-helix]] | | [[Category: Helix-turn-helix]] |
| [[Category: Metalloregulatory protein]] | | [[Category: Metalloregulatory protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:02:58 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:34:12 2008'' |
