Heidi Hu/Sandbox 1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
<Structure load='3TJ8' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
+
<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='Insert optional scene name here' />One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
-
The pathogenic bacterium [[''Helicobacter pylori'']] can colonize the human gut and has been linked to peptic ulcers and gastric carcinomas. One of the reasons that ''H. pylori'' can survive in the extremely acidic environment of the human stomach is because of the activity of a nickel-dependent enzyme, [[urease]]. The bacteria uses active urease to make ammonia and carbon dioxide from urea and water, and then uses the ammonia to neutralize its local environment. Even in a neutral environment, ''H. pylori'' makes a large quantity of premature urease, which can be quickly activated by inserting nickel into the enzyme in acid shock. However, nickel is not readily available inside the cell because free nickel can damage other cell components. As a result, a series of proteins are needed to acquire nickel and to insert the nickel into urease.
+
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 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. Transcriptional regulation activity of CsoR is only responsive to the binding of Cu(I); whereas RcnR is only responsive to the binding of Ni2+ or Co2+.
-
<scene name='Heidi_Hu/Sandbox_1/Uree_dimer_ni/1'>TextToBeDisplayed</scene>
+
[http://en.wikipedia.org/wiki/Escherichia_coli ''Escherichia coli''] RcnR blocks the transcription of nickel and cobalt efflux protein RcnA by binding to its promoter region in its apo conformation. Upon Ni(II) or Co(II)-binding, RcnR is released from the DNA allowing the transcription of RcnA and therefore the efflux of Ni2+ and Co2+.
-
One of the proteins involved in urease maturation is UreE, which functions as a nickel carrier protein.
+

Revision as of 18:29, 15 December 2011

Cu(I)-bound CsoR (PDB ID: 2HH7)

Drag the structure with the mouse to rotate
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.

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 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. Transcriptional regulation activity of CsoR is only responsive to the binding of Cu(I); whereas RcnR is only responsive to the binding of Ni2+ or Co2+.

Escherichia coli RcnR blocks the transcription of nickel and cobalt efflux protein RcnA by binding to its promoter region in its apo conformation. Upon Ni(II) or Co(II)-binding, RcnR is released from the DNA allowing the transcription of RcnA and therefore the efflux of Ni2+ and Co2+.

Proteopedia Page Contributors and Editors (what is this?)

Heidi Hu

Retrieved from "http://52.214.119.220/wiki/index.php/Heidi_Hu/Sandbox_1"
Personal tools