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| - | [[Image:2hyf.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2hyf| PDB=2hyf | SCENE= }} | | {{STRUCTURE_2hyf| PDB=2hyf | SCENE= }} |
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| - | '''The Structure of apo-MntR from Bacillus subtilis, selenomethionine derivative'''
| + | ===The Structure of apo-MntR from Bacillus subtilis, selenomethionine derivative=== |
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| - | ==Overview==
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| - | The manganese transport regulator (MntR) from Bacillus subtilis binds cognate DNA sequences in response to elevated manganese concentrations. MntR functions as a homodimer that binds two manganese ions per subunit. Metal binding takes place at the interface of the two domains that comprise each MntR subunit: an N-terminal DNA-binding domain and a C-terminal dimerization domain. In order to elucidate the link between metal binding and activation, a crystallographic study of MntR in its metal-free state has been undertaken. Here we describe the structures of the native protein and a selenomethionine-containing variant, solved to 2.8 A. The two structures contain five crystallographically unique subunits of MntR, providing diverse views of the metal-free protein. In apo-MntR, as in the manganese complex, the dimer is formed by dyad-related C-terminal domains that provide a conserved structural core. Similarly, each DNA-binding domain largely retains the folded conformation found in metal bound forms of MntR. However, compared to metal-activated MntR, the DNA-binding domains move substantially with respect to the dimer interface in apo-MntR. Overlays of multiple apo-MntR structures indicate that there is a greater range of positioning allowed between N and C-terminal domains in the metal-free state and that the DNA-binding domains of the dimer are farther apart than in the activated complex. To further investigate the conformation of the DNA-binding domain of apo-MntR, a site-directed spin labeling experiment was performed on a mutant of MntR containing cysteine at residue 6. Consistent with the crystallographic results, EPR spectra of the spin-labeled mutant indicate that tertiary structure is conserved in the presence or absence of bound metals, though slightly greater flexibility is present in inactive forms of MntR. | + | The line below this paragraph, {{ABSTRACT_PUBMED_17118401}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17118401 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17118401}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Glasfeld, A.]] | | [[Category: Glasfeld, A.]] |
| | [[Category: Transcriptional regulator]] | | [[Category: Transcriptional regulator]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:51:53 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:49:39 2008'' |
Revision as of 11:49, 28 July 2008
Template:STRUCTURE 2hyf
The Structure of apo-MntR from Bacillus subtilis, selenomethionine derivative
Template:ABSTRACT PUBMED 17118401
About this Structure
2HYF is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
The conformations of the manganese transport regulator of Bacillus subtilis in its metal-free state., DeWitt MA, Kliegman JI, Helmann JD, Brennan RG, Farrens DL, Glasfeld A, J Mol Biol. 2007 Feb 2;365(5):1257-65. Epub 2006 Oct 28. PMID:17118401
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