1q07

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[[Image:1q07.gif|left|200px]]
[[Image:1q07.gif|left|200px]]
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{{Structure
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|PDB= 1q07 |SIZE=350|CAPTION= <scene name='initialview01'>1q07</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1q07", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=AU:GOLD+ION'>AU</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= CUER ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1q07| PDB=1q07 | SCENE= }}
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|RELATEDENTRY=[[1q05|1Q05]], [[1q06|1Q06]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q07 OCA], [http://www.ebi.ac.uk/pdbsum/1q07 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q07 RCSB]</span>
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'''Crystal structure of the Au(I) form of E. coli CueR, a copper efflux regulator'''
'''Crystal structure of the Au(I) form of E. coli CueR, a copper efflux regulator'''
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[[Category: Outten, C E.]]
[[Category: Outten, C E.]]
[[Category: Xue, Y.]]
[[Category: Xue, Y.]]
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[[Category: copper efflux regulator]]
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[[Category: Copper efflux regulator]]
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[[Category: merr family transcriptional regulator]]
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[[Category: Merr family transcriptional regulator]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:42:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:07:07 2008''
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Revision as of 02:42, 3 May 2008

Template:STRUCTURE 1q07

Crystal structure of the Au(I) form of E. coli CueR, a copper efflux regulator


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

1Q07 is a Single protein structure of sequence from Escherichia coli. 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 Sat May 3 05:42:27 2008

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