Heidi Hu/Sandbox 1
From Proteopedia
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Heavy metals such as iron, nickel, copper, and zinc are important cofactors for the functions of many different metalloenzymes. High levels of these heavy metals can also cause damage cellular components, therefore intracellular levels of metals are tightly regulated within the cell. One of the ways that bacteria can regulate intracellular metal levels is by increasing the amount of metal efflux proteins. CsoR and RcnR are members of a large family of metal-responsive DNA-binding proteins, both of which regulate the transcription of metal-specific efflux proteins. CsoR is only responsive to the binding of Cu(I); whereas RcnR is only responsive to the binding of Ni(II) or Co(II). | Heavy metals such as iron, nickel, copper, and zinc are important cofactors for the functions of many different metalloenzymes. High levels of these heavy metals can also cause damage cellular components, therefore intracellular levels of metals are tightly regulated within the cell. One of the ways that bacteria can regulate intracellular metal levels is by increasing the amount of metal efflux proteins. CsoR and RcnR are members of a large family of metal-responsive DNA-binding proteins, both of which regulate the transcription of metal-specific efflux proteins. CsoR is only responsive to the binding of Cu(I); whereas RcnR is only responsive to the binding of Ni(II) or Co(II). | ||
| - | <Structure load='2HH7' size='400' frame='true' align='right' caption='Cu(I)-bound CsoR (PDB ID: [http://www.rcsb.org/pdb/explore/explore.do?structureId=2HH7 2HH7])' scene=' | + | <Structure load='2HH7' size='400' frame='true' align='right' caption='Cu(I)-bound CsoR (PDB ID: [http://www.rcsb.org/pdb/explore/explore.do?structureId=2HH7 2HH7])' scene='<scene name='Heidi_Hu/Sandbox_1/Tetrameric_csor/1'>Tetrameric CsoR</scene>' |
== RcnR and CsoR == | == RcnR and CsoR == | ||
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== CsoR Structure == | == CsoR Structure == | ||
| - | <scene name='Heidi_Hu/Sandbox_1/Tetrameric_csor/ | + | <scene name='Heidi_Hu/Sandbox_1/Tetrameric_csor/2'>Tetrameric CsoR</scene>binds one Cu(I) per monomer. The protein forms a dimer of dimers with a pore in the tetrameric interface. Each <scene name='Heidi_Hu/Sandbox_1/Tetrameric_csor/3'>Cu(I) coordinated by two different monomers</scene> of a dimer unit. Where one monomer is bound to Cu(I) by His61 and Cys65, the other monomer is bound to the metal by Cys35. [http://en.wikipedia.org/wiki/Escherichia_coli ''E. coli''] RcnR is also tetrameric and has the same protein-to-metal stochiometry. |
Revision as of 04:07, 17 December 2011
/>One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.
Introduction
Heavy metals such as iron, nickel, copper, and zinc are important cofactors for the functions of many different metalloenzymes. High levels of these heavy metals can also cause damage cellular components, therefore intracellular levels of metals are tightly regulated within the cell. One of the ways that bacteria can regulate intracellular metal levels is by increasing the amount of metal efflux proteins. CsoR and RcnR are members of a large family of metal-responsive DNA-binding proteins, both of which regulate the transcription of metal-specific efflux proteins. CsoR is only responsive to the binding of Cu(I); whereas RcnR is only responsive to the binding of Ni(II) or Co(II).
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