1q07: Difference between revisions

Revision as of 23:19, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1q07.png

Template:STRUCTURE 1q07

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

Template:ABSTRACT PUBMED 12958362

About this StructureAbout this Structure

1Q07 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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 Sun Jul 27 23:19:56 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1q07.gif|left|200px]]
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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===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_12958362}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12958362 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12958362}}
 ==About this Structure==
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 [[Category: Copper efflux regulator]]
 [[Category: Merr family transcriptional regulator]]
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