1jus: Difference between revisions

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New page: left|200px<br /><applet load="1jus" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jus, resolution 2.84Å" /> '''Crystal structure of...
 
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[[Image:1jus.jpg|left|200px]]<br /><applet load="1jus" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1jus.jpg|left|200px]]<br /><applet load="1jus" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1jus, resolution 2.84&Aring;" />
caption="1jus, resolution 2.84&Aring;" />
'''Crystal structure of the multidrug binding transcriptional repressor QacR bound to rhodamine 6G'''<br />
'''Crystal structure of the multidrug binding transcriptional repressor QacR bound to rhodamine 6G'''<br />


==Overview==
==Overview==
The Staphylococcus aureus multidrug binding protein QacR represses, transcription of the qacA multidrug transporter gene and is induced by, structurally diverse cationic lipophilic drugs. Here, we report the, crystal structures of six QacR-drug complexes. Compared to the DNA bound, structure, drug binding elicits a coil-to-helix transition that causes, induction and creates an expansive multidrug-binding pocket, containing, four glutamates and multiple aromatic and polar residues. These structures, indicate the presence of separate but linked drug-binding sites within a, single protein. This multisite drug-binding mechanism is consonant with, studies on multidrug resistance transporters.
The Staphylococcus aureus multidrug binding protein QacR represses transcription of the qacA multidrug transporter gene and is induced by structurally diverse cationic lipophilic drugs. Here, we report the crystal structures of six QacR-drug complexes. Compared to the DNA bound structure, drug binding elicits a coil-to-helix transition that causes induction and creates an expansive multidrug-binding pocket, containing four glutamates and multiple aromatic and polar residues. These structures indicate the presence of separate but linked drug-binding sites within a single protein. This multisite drug-binding mechanism is consonant with studies on multidrug resistance transporters.


==About this Structure==
==About this Structure==
1JUS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with SO4 and RHQ as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JUS OCA].  
1JUS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=RHQ:'>RHQ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JUS OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Brennan, R.G.]]
[[Category: Brennan, R G.]]
[[Category: Brown, M.H.]]
[[Category: Brown, M H.]]
[[Category: Grkovic, S.]]
[[Category: Grkovic, S.]]
[[Category: Miller, M.C.]]
[[Category: Miller, M C.]]
[[Category: Schumacher, M.A.]]
[[Category: Schumacher, M A.]]
[[Category: Skurray, R.A.]]
[[Category: Skurray, R A.]]
[[Category: RHQ]]
[[Category: RHQ]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: s. aureus]]
[[Category: s. aureus]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:35:50 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:02 2008''

Revision as of 14:27, 21 February 2008

File:1jus.jpg


1jus, resolution 2.84Å

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Crystal structure of the multidrug binding transcriptional repressor QacR bound to rhodamine 6G

OverviewOverview

The Staphylococcus aureus multidrug binding protein QacR represses transcription of the qacA multidrug transporter gene and is induced by structurally diverse cationic lipophilic drugs. Here, we report the crystal structures of six QacR-drug complexes. Compared to the DNA bound structure, drug binding elicits a coil-to-helix transition that causes induction and creates an expansive multidrug-binding pocket, containing four glutamates and multiple aromatic and polar residues. These structures indicate the presence of separate but linked drug-binding sites within a single protein. This multisite drug-binding mechanism is consonant with studies on multidrug resistance transporters.

About this StructureAbout this Structure

1JUS is a Single protein structure of sequence from Staphylococcus aureus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structural mechanisms of QacR induction and multidrug recognition., Schumacher MA, Miller MC, Grkovic S, Brown MH, Skurray RA, Brennan RG, Science. 2001 Dec 7;294(5549):2158-63. PMID:11739955

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