1q06: Difference between revisions
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|PDB= 1q06 |SIZE=350|CAPTION= <scene name='initialview01'>1q06</scene>, resolution 2.07Å | |PDB= 1q06 |SIZE=350|CAPTION= <scene name='initialview01'>1q06</scene>, resolution 2.07Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=AG:SILVER ION'>AG</scene> | |LIGAND= <scene name='pdbligand=AG:SILVER+ION'>AG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= CUER ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= CUER ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1q05|1Q05]], [[1q07|1Q07]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q06 OCA], [http://www.ebi.ac.uk/pdbsum/1q06 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q06 RCSB]</span> | |||
}} | }} | ||
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[[Category: Outten, C E.]] | [[Category: Outten, C E.]] | ||
[[Category: Xue, Y.]] | [[Category: Xue, Y.]] | ||
[[Category: copper efflux regulator]] | [[Category: copper efflux regulator]] | ||
[[Category: merr family transcriptional regulator]] | [[Category: merr family transcriptional regulator]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:07:02 2008'' | ||
Revision as of 23:07, 30 March 2008
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| , resolution 2.07Å | |||||||
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| Ligands: | |||||||
| Gene: | CUER (Escherichia coli) | ||||||
| Related: | 1Q05, 1Q07
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the Ag(I) form of E. coli CueR, a copper efflux regulator
OverviewOverview
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 StructureAbout this Structure
1Q06 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
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