Molecular Playground/CheA: Difference between revisions

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In Progress: One of the [http://www.proteopedia.org/wiki/index.php/CBI_Molecules CBI Molecules] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst].
In Progress: One of the [http://www.proteopedia.org/wiki/index.php/CBI_Molecules CBI Molecules] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst].
<Structure load='1b3q' size='500' frame='true' align='right' caption='Structure of histidine kinase CheA, [[1b3q]]' scene='User:Elizabeth_R._Haglin/Sandbox_1/P3p4p5/3'>
<Structure load='1b3q' size='500' frame='true' align='right' caption='Structure of histidine kinase CheA, [[1b3q]]' scene='User:Elizabeth_R._Haglin/Sandbox_1/P3p4p5/3'>
[[Image:Chemotaxis.png|300px|right|thumb|Chemotaxis overview <ref>PMID:15573139</ref>]]
 
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== Biological context ==
== Biological context ==
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== Structure ==
== Structure ==
[[Image:CheA_domains.png|410px|left|thumb|CheA Domains <ref>PMID: 22494339</ref>]]
 
'''CheA''' exists as a homodimer of 71-kDa subunits. Each monomer catalyzes an ATP-dependent ''trans''-phosphorylation of a histidine.  A monomer contains five domains (P1-P5 from N- to C-terminus) connected by highly dynamic linkers of various lengths.  Each domain has a distinct function.Due to the size of CheA, the solved structures available to date do not have all five domains.  The PDB files included in this proteopedia page are <u><scene name='User:Elizabeth_R._Haglin/Sandbox_1/P3p4p5/3'>1B3Q</scene></u> with a dimer of <b><font color='deepskyblue'>P3</font><font color='limegreen'>P4</font><font color='mediumorchid'>P5</font></b> and <u><scene name='User:Elizabeth_R._Haglin/Sandbox_1/P1_p2_chey/2'>2LP4</scene></u> which contains a <b><font color='gold'>P1</font><font color='hotpink'>P2</font>-<font color='red'>CheY</font></b> complex.
'''CheA''' exists as a homodimer of 71-kDa subunits. Each monomer catalyzes an ATP-dependent ''trans''-phosphorylation of a histidine.  A monomer contains five domains (P1-P5 from N- to C-terminus) connected by highly dynamic linkers of various lengths.  Each domain has a distinct function.Due to the size of CheA, the solved structures available to date do not have all five domains.  The PDB files included in this proteopedia page are <u><scene name='User:Elizabeth_R._Haglin/Sandbox_1/P3p4p5/3'>1B3Q</scene></u> with a dimer of <b><font color='deepskyblue'>P3</font><font color='limegreen'>P4</font><font color='mediumorchid'>P5</font></b> and <u><scene name='User:Elizabeth_R._Haglin/Sandbox_1/P1_p2_chey/2'>2LP4</scene></u> which contains a <b><font color='gold'>P1</font><font color='hotpink'>P2</font>-<font color='red'>CheY</font></b> complex.
*<b><font color='gold'>P1</font></b>: histidine phosphotransfer domain (HPt) mediates phosphate transfer from ATP to CheY  
*<b><font color='gold'>P1</font></b>: histidine phosphotransfer domain (HPt) mediates phosphate transfer from ATP to CheY  

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

Elizabeth R. Haglin, Michal Harel, Jaime Prilusky