1on1
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(New page: 200px<br /><applet load="1on1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1on1, resolution 1.75Å" /> '''Bacillus Subtilis Ma...)
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Revision as of 20:54, 20 November 2007
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Bacillus Subtilis Manganese Transport Regulator (Mntr) Bound To Manganese, AB Conformation.
Overview
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.
About this Structure
1ON1 is a Single protein structure of sequence from Bacillus subtilis with MN as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the manganese-bound manganese transport regulator of Bacillus subtilis., Glasfeld A, Guedon E, Helmann JD, Brennan RG, Nat Struct Biol. 2003 Aug;10(8):652-7. PMID:12847518
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