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1q09
From Proteopedia
(New page: 200px<br /><applet load="1q09" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q09, resolution 2.50Å" /> '''Crystal structure of...) |
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| - | [[Image:1q09.gif|left|200px]]<br /><applet load="1q09" size=" | + | [[Image:1q09.gif|left|200px]]<br /><applet load="1q09" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1q09, resolution 2.50Å" /> | caption="1q09, resolution 2.50Å" /> | ||
'''Crystal structure of the Zn(II) form of E. coli ZntR, a zinc-sensing transcriptional regulator (space group I4122)'''<br /> | '''Crystal structure of the Zn(II) form of E. coli ZntR, a zinc-sensing transcriptional regulator (space group I4122)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The earliest of a series of copper efflux genes in Escherichia coli are | + | 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== | ||
| - | 1Q09 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 SO4 and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1Q09 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=SO4:'>SO4</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q09 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Changela, A.]] | [[Category: Changela, A.]] | ||
[[Category: Chen, K.]] | [[Category: Chen, K.]] | ||
| - | [[Category: Halloran, T | + | [[Category: Halloran, T V.O.]] |
[[Category: Holschen, J.]] | [[Category: Holschen, J.]] | ||
[[Category: Mondragon, A.]] | [[Category: Mondragon, A.]] | ||
| - | [[Category: Outten, C | + | [[Category: Outten, C E.]] |
[[Category: Xue, Y.]] | [[Category: Xue, Y.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
| Line 25: | Line 25: | ||
[[Category: zn(ii)-responsive regulator of znta]] | [[Category: zn(ii)-responsive regulator of znta]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:27 2008'' |
Revision as of 12:34, 21 February 2008
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Crystal structure of the Zn(II) form of E. coli ZntR, a zinc-sensing transcriptional regulator (space group I4122)
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.
About this Structure
1Q09 is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR., Changela A, Chen K, Xue Y, Holschen J, Outten CE, O'Halloran TV, Mondragon A, Science. 2003 Sep 5;301(5638):1383-7. PMID:12958362
Page seeded by OCA on Thu Feb 21 14:34:27 2008
