1q08: Difference between revisions

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New page: left|200px<br /><applet load="1q08" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q08, resolution 1.90Å" /> '''Crystal structure of...
 
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[[Image:1q08.gif|left|200px]]<br /><applet load="1q08" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1q08.gif|left|200px]]<br /><applet load="1q08" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1q08, resolution 1.90&Aring;" />
caption="1q08, resolution 1.90&Aring;" />
'''Crystal structure of the Zn(II) form of E. coli ZntR, a zinc-sensing transcriptional regulator, at 1.9 A resolution (space group P212121)'''<br />
'''Crystal structure of the Zn(II) form of E. coli ZntR, a zinc-sensing transcriptional regulator, at 1.9 A resolution (space group P212121)'''<br />


==Overview==
==Overview==
The earliest of a series of copper efflux genes in Escherichia coli are, controlled by CueR, a member of the MerR family of transcriptional, activators. Thermodynamic calibration of CueR reveals a zeptomolar, (10(-21) molar) sensitivity to free Cu+, which is far less than one atom, per cell. Atomic details of this extraordinary sensitivity and selectivity, for +1transition-metal ions are revealed by comparing the crystal, structures of CueR and a Zn2+-sensing homolog, ZntR. An unusual buried, metal-receptor site in CueR restricts the metal to a linear, two-coordinate geometry and uses helix-dipole and hydrogen-bonding, interactions to enhance metal binding. This binding mode is rare among, metalloproteins but well suited for an ultrasensitive genetic switch.
The earliest of a series of copper efflux genes in Escherichia coli are controlled by CueR, a member of the MerR family of transcriptional activators. Thermodynamic calibration of CueR reveals a zeptomolar (10(-21) molar) sensitivity to free Cu+, which is far less than one atom per cell. Atomic details of this extraordinary sensitivity and selectivity for +1transition-metal ions are revealed by comparing the crystal structures of CueR and a Zn2+-sensing homolog, ZntR. An unusual buried metal-receptor site in CueR restricts the metal to a linear, two-coordinate geometry and uses helix-dipole and hydrogen-bonding interactions to enhance metal binding. This binding mode is rare among metalloproteins but well suited for an ultrasensitive genetic switch.


==About this Structure==
==About this Structure==
1Q08 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4, ZN and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q08 OCA].  
1Q08 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q08 OCA].  


==Reference==
==Reference==
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[[Category: Changela, A.]]
[[Category: Changela, A.]]
[[Category: Chen, K.]]
[[Category: Chen, K.]]
[[Category: Halloran, T.V.O.]]
[[Category: Halloran, T V.O.]]
[[Category: Holschen, J.]]
[[Category: Holschen, J.]]
[[Category: Mondragon, A.]]
[[Category: Mondragon, A.]]
[[Category: Outten, C.E.]]
[[Category: Outten, C E.]]
[[Category: Xue, Y.]]
[[Category: Xue, Y.]]
[[Category: MG]]
[[Category: MG]]
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[[Category: zn(ii)-responsive regulator of znta]]
[[Category: zn(ii)-responsive regulator of znta]]


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