2bow
From Proteopedia
(New page: 200px<br /><applet load="2bow" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bow, resolution 2.8Å" /> '''MULTIDRUG-BINDING DOM...) |
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| - | [[Image:2bow.jpg|left|200px]]<br /><applet load="2bow" size=" | + | [[Image:2bow.jpg|left|200px]]<br /><applet load="2bow" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bow, resolution 2.8Å" /> | caption="2bow, resolution 2.8Å" /> | ||
'''MULTIDRUG-BINDING DOMAIN OF TRANSCRIPTION ACTIVATOR BMRR IN COMPLEX WITH A LIGAND, TETRAPHENYLPHOSPHONIUM'''<br /> | '''MULTIDRUG-BINDING DOMAIN OF TRANSCRIPTION ACTIVATOR BMRR IN COMPLEX WITH A LIGAND, TETRAPHENYLPHOSPHONIUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Multidrug-efflux transporters demonstrate an unusual ability to recognize | + | Multidrug-efflux transporters demonstrate an unusual ability to recognize multiple structurally dissimilar toxins. A comparable ability to bind diverse hydrophobic cationic drugs is characteristic of the Bacillus subtilis transcription regulator BmrR, which upon drug binding activates expression of the multidrug transporter Bmr. Crystal structures of the multidrug-binding domain of BmrR (2.7 A resolution) and of its complex with the drug tetraphenylphosphonium (2.8 A resolution) revealed a drug-induced unfolding and relocation of an alpha helix, which exposes an internal drug-binding pocket. Tetraphenylphosphonium binding is mediated by stacking and van der Waals contacts with multiple hydrophobic residues of the pocket and by an electrostatic interaction between the positively charged drug and a buried glutamate residue, which is the key to cation selectivity. Similar binding principles may be used by other multidrug-binding proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 2BOW 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, SO4 and P4P as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2BOW 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>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=P4P:'>P4P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BOW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brennan, R | + | [[Category: Brennan, R G.]] |
| - | [[Category: Markham, P | + | [[Category: Markham, P N.]] |
| - | [[Category: Neyfakh, A | + | [[Category: Neyfakh, A A.]] |
| - | [[Category: Zheleznova, E | + | [[Category: Zheleznova, E E.]] |
[[Category: MN]] | [[Category: MN]] | ||
[[Category: P4P]] | [[Category: P4P]] | ||
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[[Category: transcription activator]] | [[Category: transcription activator]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:02 2008'' |
Revision as of 14:40, 21 February 2008
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MULTIDRUG-BINDING DOMAIN OF TRANSCRIPTION ACTIVATOR BMRR IN COMPLEX WITH A LIGAND, TETRAPHENYLPHOSPHONIUM
Overview
Multidrug-efflux transporters demonstrate an unusual ability to recognize multiple structurally dissimilar toxins. A comparable ability to bind diverse hydrophobic cationic drugs is characteristic of the Bacillus subtilis transcription regulator BmrR, which upon drug binding activates expression of the multidrug transporter Bmr. Crystal structures of the multidrug-binding domain of BmrR (2.7 A resolution) and of its complex with the drug tetraphenylphosphonium (2.8 A resolution) revealed a drug-induced unfolding and relocation of an alpha helix, which exposes an internal drug-binding pocket. Tetraphenylphosphonium binding is mediated by stacking and van der Waals contacts with multiple hydrophobic residues of the pocket and by an electrostatic interaction between the positively charged drug and a buried glutamate residue, which is the key to cation selectivity. Similar binding principles may be used by other multidrug-binding proteins.
About this Structure
2BOW is a Single protein structure of sequence from Bacillus subtilis with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter., Zheleznova EE, Markham PN, Neyfakh AA, Brennan RG, Cell. 1999 Feb 5;96(3):353-62. PMID:10025401
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