2v9a: Difference between revisions

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[[Image:2v9a.~~jpg~~|left|200px]]

[[Image:2v9a.png|left|200px]]

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~~'''~~STRUCTURE OF CITRATE-FREE PERIPLASMIC DOMAIN OF SENSOR HISTIDINE KINASE CITA~~'''~~

===STRUCTURE OF CITRATE-FREE PERIPLASMIC DOMAIN OF SENSOR HISTIDINE KINASE CITA===

~~==Overview==~~

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~~Sensor histidine kinases of two~~-~~component signal~~-~~transduction systems are essential for bacteria to adapt to variable environmental conditions. However~~, ~~despite their prevalence~~, it ~~is not well understood how extracellular signals such as ligand binding regulate the activity of these sensor kinases~~. ~~CitA~~ is the ~~sensor histidine kinase in Klebsiella pneumoniae that regulates the transport and anaerobic metabolism of citrate in response to its extracellular concentration~~. ~~We report here the X-ray structures of the periplasmic sensor domain of CitA in the citrate~~-~~free and citrate~~-bound states. A comparison of the two structures shows that ligand binding causes a considerable contraction of the sensor domain. This contraction may represent the molecular switch that activates transmembrane signaling in the receptor.

The line below this paragraph, {{ABSTRACT_PUBMED_18258261}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18258261 is the PubMed ID number.

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==About this Structure==

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[[Category: Transmembrane]]

[[Category: Two-component regulatory system]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 18~~:24:52 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:25:57 2008''

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-[[Image:2v9a.jpg|left|200px]]
+{{Seed}}
+[[Image:2v9a.png|left|200px]]
 <!--
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 {{STRUCTURE_2v9a|  PDB=2v9a  |  SCENE=  }}
-'''STRUCTURE OF CITRATE-FREE PERIPLASMIC DOMAIN OF SENSOR HISTIDINE KINASE CITA'''
+===STRUCTURE OF CITRATE-FREE PERIPLASMIC DOMAIN OF SENSOR HISTIDINE KINASE CITA===
-==Overview==
+<!--
-Sensor histidine kinases of two-component signal-transduction systems are essential for bacteria to adapt to variable environmental conditions. However, despite their prevalence, it is not well understood how extracellular signals such as ligand binding regulate the activity of these sensor kinases. CitA is the sensor histidine kinase in Klebsiella pneumoniae that regulates the transport and anaerobic metabolism of citrate in response to its extracellular concentration. We report here the X-ray structures of the periplasmic sensor domain of CitA in the citrate-free and citrate-bound states. A comparison of the two structures shows that ligand binding causes a considerable contraction of the sensor domain. This contraction may represent the molecular switch that activates transmembrane signaling in the receptor.
+The line below this paragraph, {{ABSTRACT_PUBMED_18258261}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18258261 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18258261}}
 ==About this Structure==
@@ Line 43: / Line 47: @@
 [[Category: Transmembrane]]
 [[Category: Two-component regulatory system]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:24:52 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:25:57 2008''