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| - | [[Image:2f5c.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2f5c.png|left|200px]] |
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| | {{STRUCTURE_2f5c| PDB=2f5c | SCENE= }} | | {{STRUCTURE_2f5c| PDB=2f5c | SCENE= }} |
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| - | '''Bacillus subtilis Manganese transport regulator (MNTR) bound to manganese, hexagonal crystal form'''
| + | ===Bacillus subtilis Manganese transport regulator (MNTR) bound to manganese, hexagonal crystal form=== |
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| - | ==Overview==
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| - | The manganese transport regulator (MntR) of Bacillus subtilis is activated by Mn(2+) to repress transcription of genes encoding transporters involved in the uptake of manganese. MntR is also strongly activated by cadmium, both in vivo and in vitro, but it is poorly activated by other metal cations, including calcium and zinc. The previously published MntR.Mn(2+) structure revealed a binuclear complex of manganese ions with a metal-metal separation of 3.3 A (herein designated the AB conformer). Analysis of four additional crystal forms of MntR.Mn(2+) reveals that the AB conformer is only observed in monoclinic crystals at 100 K, suggesting that this conformation may be stabilized by crystal packing forces. In contrast, monoclinic crystals analyzed at room temperature (at either pH 6.5 or pH 8.5), and a second hexagonal crystal form (analyzed at 100 K), all reveal the shift of one manganese ion by 2.5 A, thereby leading to a newly identified conformation (the AC conformer) with an internuclear distance of 4.4 A. Significantly, the cadmium and calcium complexes of MntR also contain binuclear complexes with a 4.4 A internuclear separation. In contrast, the zinc complex of MntR contains only one metal ion per subunit, in the A site. Isothermal titration calorimetry confirms the stoichiometry of Mn(2+), Cd(2+), and Zn(2+) binding to MntR. We propose that the specificity of MntR activation is tied to productive binding of metal ions at two sites; the A site appears to act as a selectivity filter, determining whether the B or C site will be occupied and thereby fully activate MntR. | + | The line below this paragraph, {{ABSTRACT_PUBMED_16533030}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16533030 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16533030}} |
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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 Sun May 4 03:28:46 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:03:15 2008'' |
Revision as of 11:03, 27 July 2008
Template:STRUCTURE 2f5c
Bacillus subtilis Manganese transport regulator (MNTR) bound to manganese, hexagonal crystal form
Template:ABSTRACT PUBMED 16533030
About this Structure
2F5C is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structural basis for the metal-selective activation of the manganese transport regulator of Bacillus subtilis., Kliegman JI, Griner SL, Helmann JD, Brennan RG, Glasfeld A, Biochemistry. 2006 Mar 21;45(11):3493-505. PMID:16533030
Page seeded by OCA on Sun Jul 27 14:03:15 2008
