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 1.75&Aring;" /> '''Bacillus Subtilis Ma...)
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[[Image:1on1.jpg|left|200px]]<br /><applet load="1on1" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1on1, resolution 1.75&Aring;" />
caption="1on1, resolution 1.75&Aring;" />
'''Bacillus Subtilis Manganese Transport Regulator (Mntr) Bound To Manganese, AB Conformation.'''<br />
'''Bacillus Subtilis Manganese Transport Regulator (Mntr) Bound To Manganese, AB Conformation.'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1ON1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ON1 OCA].
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1ON1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ON1 OCA].
==Reference==
==Reference==
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Brennan, R.G.]]
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[[Category: Brennan, R G.]]
[[Category: Glasfeld, A.]]
[[Category: Glasfeld, A.]]
[[Category: Guedon, E.]]
[[Category: Guedon, E.]]
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[[Category: Helmann, J.D.]]
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[[Category: Helmann, J D.]]
[[Category: MN]]
[[Category: MN]]
[[Category: dna-binding protein]]
[[Category: dna-binding protein]]
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[[Category: metalloregulatory protein]]
[[Category: metalloregulatory protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:01:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:28 2008''

Revision as of 12:19, 21 February 2008


1on1, resolution 1.75Å

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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 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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